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Human Metabolome Database Version 2.5

 

Showing metabocard for L-Carnitine (HMDB00062)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-05-28 10:25:23
Accession Number HMDB00062
Secondary Accession Numbers HMDB01467
Common Name L-Carnitine
Description Carnitine is not an essential amino acid; it can be synthesized in the body. However, it is so important in providing energy to muscles including the heart-that some researchers are now recommending carnitine supplements in the diet, particularly for people who do not consume much red meat, the main food source for carnitine. Carnitine has been described as a vitamin, an amino acid, or a metabimin, i.e., an essential metabolite. Like the B vitamins, carnitine contains nitrogen and is very soluble in water, and to some researchers carnitine is a vitamin (Liebovitz 1984). It was found that an animal (yellow mealworm) could not grow without carnitine in its diet. However, as it turned out, almost all other animals, including humans, do make their own carnitine; thus, it is no longer considered a vitamin. Nevertheless, in certain circumstances-such as deficiencies of methionine, lysine or vitamin C or kidney dialysis--carnitine shortages develop. Under these conditions, carnitine must be absorbed from food, and for this reason it is sometimes referred to as a "metabimin" or a conditionally essential metabolite. Like the other amino acids used or manufactured by the body, carnitine is an amine. But like choline, which is sometimes considered to be a B vitamin, carnitine is also an alcohol (specifically, a trimethylated carboxy-alcohol). Thus, carnitine is an unusual amino acid and has different functions than most other amino acids, which are most usually employed by the body in the construction of protein. Carnitine is an essential factor in fatty acid metabolism in mammals. It's most important known metabolic function is to transport fat into the mitochondria of muscle cells, including those in the heart, for oxidation. This is how the heart gets most of its energy. In humans, about 25% of carnitine is synthesized in the liver, kidney and brain from the amino acids lysine and methionine. Most of the carnitine in the body comes from dietary sources such as red meat and dairy products. Inborn errors of carnitine metabolism can lead to brain deterioration like that of Reye's syndrome, gradually worsening muscle weakness, Duchenne-like muscular dystrophy and extreme muscle weakness with fat accumulation in muscles. Borurn et al. (1979) describe carnitine as an essential nutrient for pre-term babies, certain types (non-ketotic) of hypoglycemics, kidney dialysis patients, cirrhosis, and in kwashiorkor, type IV hyperlipidemia, heart muscle disease (cardiomyopathy), and propionic or organic aciduria (acid urine resulting from genetic or other anomalies). In all these conditions and the inborn errors of carnitine metabolism, carnitine is essential to life and carnitine supplements are valuable. carnitine therapy may also be useful in a wide variety of clinical conditions. carnitine supplementation has improved some patients who have angina secondary to coronary artery disease. It may be worth a trial in any form of hyperlipidemia or muscle weakness. carnitine supplements may be useful in many forms of toxic or metabolic liver disease and in cases of heart muscle disease. Hearts undergoing severe arrhythmia quickly deplete their stores of carnitine. Athletes, particularly in Europe, have used carnitine supplements for improved endurance. carnitine may improve muscle building by improving fat utilization and may even be useful in treating obesity. carnitine joins a long list of nutrients which may be of value in treating pregnant women, hypothyroid individuals, and male infertility due to low motility of sperm. Even the Physician's Desk Reference gives indication for carnitine supplements as "improving the tolerance of ischemic heart disease, myocardial insufficiencies, and type IV hyperlipoproteinemia. carnitine deficiency is noted in abnormal liver function, renal dialysis patients, and severe to moderate muscular weakness with associated anorexia." (http://www.dcnutrition.com)
Synonyms
  1. (-)-(R)-3-Hydroxy-4-(trimethylammonio)butyrate
  2. (-)-carnitine
  3. (R)-(3-Carboxy-2-hydroxypropyl)trimethylammonium hydroxide
  4. (r)-carnitine
  5. (s)-carnitine
  6. 1-carnitine
  7. 3-carboxy-2-hydroxy-N,N,N-trimethyl-1-propanaminium
  8. Bicarnesine
  9. Carnilean
  10. Carnitene
  11. Carnitine
  12. Carnitor
  13. D-carnitine
  14. delta-carnitine
  15. DL-carnitine
  16. Gamma-trimethyl-ammonium-beta-hydroxybutirate
  17. Gamma-trimethyl-beta-hydroxybutyrobetaine
  18. Gamma-trimethyl-hydroxybutyrobetaine
  19. Karnitin
  20. L-(-)-carnitine
  21. L-carnitine
  22. L-gamma-trimethyl-beta-hydroxybutyrobetaine
  23. Levocarnitina
  24. Levocarnitine
  25. Levocarnitinum
  26. R-(-)-3-hydroxy-4-trimethylaminobutyrate
  27. Vitamin BT
  28. Carniking
  29. Carniking 50
  30. Carnipass
  31. Carnipass 20
  32. 3-hydroxy-4-trimethylammoniobutanoate
  33. 3-hydroxy-4-trimethylammoniobutanoic acid
Chemical IUPAC Name (3R)-3-hydroxy-4-trimethylammonio-butanoate
Chemical Formula C7H15NO3
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Amino acids and Amino Acid conjugates
Class
  • Quaternary Amines
  • Amino Acids
Sub Class
  • Short chain acyl carnitines
Family
  • Mammalian Metabolite
Species
  • cation
  • anion
  • secondary alcohol
  • quaternary ammonium salt
  • carboxylic acid salt
Biofunction
  • Essential amino acid
  • Component of Alanine and aspartate metabolism
  • Component of Fatty acid metabolism
Application
—
Source
  • Endogenous
Average Molecular Weight 161.199
Monoisotopic Molecular Weight 161.105194
Isomeric SMILES C[N+](C)(C)C[C@@H](O)CC([O-])=O
Canonical SMILES C[N+](C)(C)CC(O)CC([O-])=O
KEGG Compound ID C00318 Link Image
BioCyc ID CARNITINE Link Image
BiGG ID 34600 Link Image
Wikipedia Link L-Carnitine Link Image
NuGOwiki Link HMDB00062 Link Image
Metagene Link HMDB00062 Link Image
METLIN ID 52 Link Image
PubChem Compound 2724480 Link Image
PubChem Substance 8787949 Link Image
ChEBI ID 16347 Link Image
CAS Registry Number 541-15-1
InChI Identifier InChI=1/C7H15NO3/c1-8(2,3)5-6(9)4-7(10)11/h6,9H,4-5H2,1-3H3/t6-/m0/s1
Synthesis Reference Bols, Mikael; Lundt, Inge; Pedersen, Christian. Simple synthesis of (R)-carnitine from D-galactono-1,4-lactone. Tetrahedron (1992), 48(2), 319-24.
Melting Point (Experimental) 197 oC
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 1000 mg/mL at 25 oC [MEYLAN,WM et al. (1996)]; 5.33 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge 0
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -2.90 [Predicted by ALOGPS]; -5.48 [MEYLAN,WM & HOWARD,PH (1995)] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID 1NDF Link Image
Experimental PDB File Show
Experimental PDB Structure
Experimental 1H NMR Spectrum Download Spectrum
Download FID (Varian)
Show Experimental Conditions Link Image
Experimental 13C NMR Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Experimental 13C HSQC Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum
Low Energy
Download File
Show Experimental Conditions Link Image
Medium Energy
Download File
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High Energy
Download File
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Simplified TOCSY Spectrum Show Image
Show Peaklist
BMRB Spectrum Show Image
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Cellular Location
  • Cytoplasm
  • Mitochondria
  • endoplasmic reticulum
  • Extracellular
  • peroxisome
Biofluid Location
  • Blood
  • Cerebrospinal Fluid
  • Urine
Tissue Location
Tissue References
Adipose Tissue —
Bladder —
Brain —
Erythrocyte —
Fibroblasts —
Intestine —
Kidney —
Liver —
Lung —
Muscle —
Myocardium —
Nerve Cells —
Neuron —
Platelet —
Skeletal Muscle —
Sperm —
Testes —
Concentrations (Normal)
Biofluid Blood
Value 43.0 (26.0-79.0) uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Shihabi ZK, Oles KS, McCormick CP, Penry JK: Serum and tissue carnitine assay based on dialysis. Clin Chem. 1992 Aug;38(8 Pt 1):1414-7. [PubMed Link Image]
Biofluid Blood
Value 33.6 +/- 6.2 uM
Age Children:1-13 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp., Basel, Switzerland c1981-1992.
Biofluid Blood
Value 38.2 +/- 5.4 uM
Age Adult:>18 yrs old
Sex Female
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp., Basel, Switzerland c1981-1992.
Biofluid CSF
Value 4.0 (2.0 - 9.0) uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Shihabi ZK, Oles KS, McCormick CP, Penry JK: Serum and tissue carnitine assay based on dialysis. Clin Chem. 1992 Aug;38(8 Pt 1):1414-7. [PubMed Link Image]
Biofluid CSF
Value 1.900 +/- 0.474 uM
Age Adult:>18 yrs old
Sex N/A
Patient information Normal
Comments Not Available
References
Biofluid Urine
Value 23.5 +/- 4.0 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Male
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by Cornelius Lentner.
  • West Cadwell, N.J. : Medical education Div., Ciba-Geigy Corp.
  • Basel, Switzerland c1981-1992.
Biofluid Urine
Value 18.0 +/- 1.2 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Female
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by Cornelius Lentner.
  • West Cadwell, N.J. : Medical education Div., Ciba-Geigy Corp.
  • Basel, Switzerland c1981-1992.
Biofluid Urine
Value 57 +/- 5 uM
Age Adult:>18 yrs old
Sex Male
Patient information Normal
Comments Not Available
References
  • Shaykhutdinov RA, MacInnis GD, Dowlatabadi R, Weljie AM, Vogel HJ. Quantitative analysis of metabolite concentrations in human urine samples using 13C{1H} NMR spectroscopy. Metabolomics. 2009
Concentrations (Abnormal)
Biofluid Urine
Value 13.3 (11.6-15.1) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Condition Diabetes mellitus type 2
Comments With ketoacidosis,
References
  • Hoppel CL, Genuth SM: Urinary excretion of acetylcarnitine during human diabetic and fasting ketosis. Am J Physiol. 1982 Aug;243(2):E168-72. [PubMed Link Image]
Biofluid Urine
Value 41.3 (38.3-44.2) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Condition Diabetes mellitus type 2
Comments With ketoacidosis
References
  • Hoppel CL, Genuth SM: Urinary excretion of acetylcarnitine during human diabetic and fasting ketosis. Am J Physiol. 1982 Aug;243(2):E168-72. [PubMed Link Image]
Biofluid Urine
Value 7.0 (0.0-30.0) umol/mmol creatinine
Age N/A
Sex Both
Condition Lung Cancer
Comments Not Available
References
  • HMP experimental
Associated Disorders
Condition References
Diabetes mellitus type 2
  • Hoppel CL, Genuth SM: Urinary excretion of acetylcarnitine during human diabetic and fasting ketosis. Am J Physiol. 1982 Aug;243(2):E168-72. [PubMed Link Image]
Lung Cancer
  • HMP experimental
OMIM ID
Pathways
Name SMPDB Link KEGG Link
Beta Oxidation of Very Long Chain Fatty Acids SMP00052 Link Image map01040 Link Image
Carnitine Synthesis SMP00465 Link Image
Mitochondrial Beta-Oxidation of Long Chain Saturated Fatty Acids SMP00482 Link Image
Mitochondrial Beta-Oxidation of Short Chain Saturated Fatty Acids SMP00480 Link Image
Oxidation of Branched Chain Fatty Acids SMP00030 Link Image
General References
  1. Wachter S, Vogt M, Kreis R, Boesch C, Bigler P, Hoppeler H, Krahenbuhl S: Long-term administration of L-carnitine to humans: effect on skeletal muscle carnitine content and physical performance. Clin Chim Acta. 2002 Apr;318(1-2):51-61. [PubMed Link Image]
  2. Evans AM, Fornasini G: Pharmacokinetics of L-carnitine. Clin Pharmacokinet. 2003;42(11):941-67. [PubMed Link Image]
  3. Pastoris O, Dossena M, Foppa P, Catapano M, Arbustini E, Bellini O, Dal Bello B, Minzioni G, Ceriana P, Barzaghi N: Effect of L-carnitine on myocardial metabolism: results of a balanced, placebo-controlled, double-blind study in patients undergoing open heart surgery. Pharmacol Res. 1998 Feb;37(2):115-22. [PubMed Link Image]
  4. Stephens FB, Constantin-Teodosiu D, Laithwaite D, Simpson EJ, Greenhaff PL: Insulin stimulates L-carnitine accumulation in human skeletal muscle. FASEB J. 2006 Feb;20(2):377-9. Epub 2005 Dec 20. [PubMed Link Image]
  5. Tamai I, China K, Sai Y, Kobayashi D, Nezu J, Kawahara E, Tsuji A: Na(+)-coupled transport of L-carnitine via high-affinity carnitine transporter OCTN2 and its subcellular localization in kidney. Biochim Biophys Acta. 2001 Jun 6;1512(2):273-84. [PubMed Link Image]
  6. Malaguarnera M, Pistone G, Astuto M, Dell'Arte S, Finocchiaro G, Lo Giudice E, Pennisi G: L-Carnitine in the treatment of mild or moderate hepatic encephalopathy. Dig Dis. 2003;21(3):271-5. [PubMed Link Image]
  7. Oey NA, van Vlies N, Wijburg FA, Wanders RJ, Attie-Bitach T, Vaz FM: L-carnitine is synthesized in the human fetal-placental unit: potential roles in placental and fetal metabolism. Placenta. 2006 Aug;27(8):841-6. Epub 2005 Nov 18. [PubMed Link Image]
  8. Feinfeld DA, Kurian P, Cheng JT, Dilimetin G, Arriola MR, Ward L, Manis T, Carvounis CP: Effect of oral L-carnitine on serum myoglobin in hemodialysis patients. Ren Fail. 1996 Jan;18(1):91-6. [PubMed Link Image]
  9. Matalliotakis I, Koumantaki Y, Evageliou A, Matalliotakis G, Goumenou A, Koumantakis E: L-carnitine levels in the seminal plasma of fertile and infertile men: correlation with sperm quality. Int J Fertil Womens Med. 2000 May-Jun;45(3):236-40. [PubMed Link Image]
  10. Vescovo G, Ravara B, Gobbo V, Dalla Libera L: Inflammation and perturbation of the l-carnitine system in heart failure. Eur J Heart Fail. 2005 Oct;7(6):997-1002. [PubMed Link Image]
  11. Lerch R: [The effect of L-carnitine on ischemic heart disease: experimental results] Schweiz Rundsch Med Prax. 1998 Jan 21;87(4):97-100. [PubMed Link Image]
  12. Khademi A, Alleyassin A, Safdarian L, Hamed EA, Rabiee E, Haghaninezhad H: The effects of L-carnitine on sperm parameters in smoker and non-smoker patients with idiopathic sperm abnormalities. J Assist Reprod Genet. 2005 Dec;22(11-12):395-9. [PubMed Link Image]
  13. Stradomska TJ, Tylki-Szymanska A, Bentkowski Z: Very long-chain fatty acids in Rett syndrome. Eur J Pediatr. 1999 Mar;158(3):226-9. [PubMed Link Image]
  14. Hoppel CL, Genuth SM: Urinary excretion of acetylcarnitine during human diabetic and fasting ketosis. Am J Physiol. 1982 Aug;243(2):E168-72. [PubMed Link Image]
  15. Waldner R, Laschan C, Lohninger A, Gessner M, Tuchler H, Huemer M, Spiegel W, Karlic H: Effects of doxorubicin-containing chemotherapy and a combination with L-carnitine on oxidative metabolism in patients with non-Hodgkin lymphoma. J Cancer Res Clin Oncol. 2006 Feb;132(2):121-8. Epub 2005 Nov 8. [PubMed Link Image]
  16. Lenzi A, Sgro P, Salacone P, Paoli D, Gilio B, Lombardo F, Santulli M, Agarwal A, Gandini L: A placebo-controlled double-blind randomized trial of the use of combined l-carnitine and l-acetyl-carnitine treatment in men with asthenozoospermia. Fertil Steril. 2004 Jun;81(6):1578-84. [PubMed Link Image]
  17. Sinclair C, Gilchrist JM, Hennessey JV, Kandula M: Muscle carnitine in hypo- and hyperthyroidism. Muscle Nerve. 2005 Sep;32(3):357-9. [PubMed Link Image]
  18. Ahmad S: L-carnitine in dialysis patients. Semin Dial. 2001 May-Jun;14(3):209-17. [PubMed Link Image]
  19. Shihabi ZK, Oles KS, McCormick CP, Penry JK: Serum and tissue carnitine assay based on dialysis. Clin Chem. 1992 Aug;38(8 Pt 1):1414-7. [PubMed Link Image]
  20. Wikipedia Link Image
Metabolic Enzymes
  1. Carnitine O-acetyltransferase
  2. Peroxisomal carnitine O-octanoyltransferase
  3. Carnitine O-palmitoyltransferase I, muscle isoform
  4. Carnitine O-palmitoyltransferase I, liver isoform
  5. Carnitine O-palmitoyltransferase 2, mitochondrial precursor
  6. Carnitine O-palmitoyltransferase I, brain isoform
  7. Gamma-butyrobetaine dioxygenase
  8. Organic cation/carnitine transporter 2
  9. Organic cation/carnitine transporter 1
  10. Mitochondrial carnitine/acylcarnitine carrier protein
  11. Solute carrier family 22
  12. Carnitine O-octanoyltransferase
  13. cDNA, FLJ93082, Homo sapiens carnitine palmitoyltransferase II (CPT2), nuclear geneencoding mitochondrial protein, mRNA (Carnitine palmitoyltransferase II)
  14. Mitochondrial carnitine/acylcarnitine carrier protein CACL
Enzyme 1 [top]
Enzyme 1 ID 5257
Enzyme 1 Name Carnitine O-acetyltransferase
Enzyme 1 Synonyms
  1. Carnitine acetylase
  2. CAT
  3. Carnitine acetyltransferase
  4. CrAT
Enzyme 1 Gene Name CRAT
Enzyme 1 Protein Sequence >Carnitine O-acetyltransferase 
MLAFAARTVVKPLGFLKPFSLMKASSRFKAHQDALPRLPVPPLQQSLDHYLKALQPIVSE
EEWAHTKQLVDEFQASGGVGERLQKGLERRARKTENWLSEWWLKTAYLQYRQPVVIYSSP
GVMLPKQDFVDLQGQLRFAAKLIEGVLDFKVMIDNETLPVEYLGGKPLCMNQYYQILSSC
RVPGPKQDTVSNFSKTKKPPTHITVVHNYQFFELDVYHSDGTPLTADQIFVQLEKIWNSS
LQTNKEPVGILTSNHRNSWAKAYNTLIKDKVNRDSVRSIQKSIFTVCLDATMPRVSEDVY
RSHVAGQMLHGGGSRLNSGNRWFDKTLQFIVAEDGSCGLVYEHAAAEGFPIVTLLDYVIE
YTKKPELVRSPMVPLPMPKKLRFNITPEIKSDIEKAKQNLSIMIQDLDITVMVFHHFGKD
FPKSEKLSPDAFIQMALQLAYYRIYGQACATYESASLRMFHLGRTDTIRSASMDSLTFVK
AMDDSSVTEHQKVELLRKAVQAHRGYTDRAIRGEAFDRHLLGLKLQAIEDLVSMPDIFMD
TSYAIAMHFHLSTSQVPAKTDCVMFFGPVVPDGYGVCYNPMEAHINFSLSAYNSCAETNA
ARLAHYLEKALLDMRALLQSHPRAKL
Enzyme 1 Number of Residues 626
Enzyme 1 Molecular Weight 70927
Enzyme 1 Theoretical pI 8.63
Enzyme 1 GO Classification
Function
  • acyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring groups other than amino-acyl groups
Process
—
Component
—
Enzyme 1 General Function Not Available
Enzyme 1 Specific Function Carnitine acetylase is specific for short chain fatty acids. Carnitine acetylase seems to affect the flux through the pyruvate dehydrogenase complex. It may be involved as well in the transport of acetyl-CoA into mitochondria
Enzyme 1 Pathways Not Available
Enzyme 1 Reactions
  • acetyl-CoA + carnitine = CoA + O-acetylcarnitine
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • 1-16
Enzyme 1 Transmembrane Regions Not Available
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 927415 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P43155 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name CACP_HUMAN Link Image
Enzyme 1 PDB ID 1S5O Link Image
Enzyme 1 PDB File Show
Enzyme 1 3D Structure
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1876 bp 
AGCCTTCGCTGCCAGGACCGTGGTGAAGCCTCTGGGCTTCCTGAAGCCCTTCTCCTTGAT
GAAGGCTTCCAGCCGCTTCAAGGCACACCAGGATGCCCTGCCACGGCTGCCCGTGCCCCC
TCTCCAGCAGTCCCTGGACCACTACCTGAAGGCGCTGCAGCCCATCGTGAGTGAGGAGGA
GTGGGCCCACACCAAGCAGCTGGTGGATGAGTTTCAGGCCTCAGGAGGTGTAGGGGAGCG
CCTGCAGAAGGGGCTGGGGCGTCGGGCCAGGAAGACGGAGAACTGGCTGTCTGAGTGGTG
GCTCAAGACCGCCTACCTCCAGTACCGCCAGCCTGTGGTCATCTACTCGAGCCCAGGCGT
GATGCTACCCAAGCAGGACTTCGTGGACCTGCAGGGTCAGCTCCGATTTGCTGCCAAACT
CATTGAGGGTGTGTTGGATTTCAAGGTCATGATTGACAACGAGACCCTGCCCGTGGAGTA
CCTGGNGGGGAAGCCACTGTGCATGAACCAGTACTATCAGATCTTGTCCTCCTGCCGAGT
GCCGGGCCCCAAGCAGGACACAGTCAGCAACTTCAGCAAGACCAAGAAGCCTCCCACGCA
CATCACCGTGGTACACAACTACCAGTTTTTTGAGCTGGATGTGTACCACAGTGACGGGAC
ACCCCTCACTGCGGATCAGATCTTTGTGCAGCTGGAGAAGATCTGGAACTCATCCCTACA
GACCAACAAGGAGCCTGTGGGCATCCTCACCTCCAACCACCGCAACTCCTGGGCCAAGGC
ATACAACACCCTCATCAAAGACAAGGTGAACCGGGATTCCGTGCGCTCCATCCAGAAGAG
CATCTTCACCGTGTGCCTAGATGCAACCATGCCCAGGGTCTCAGAAGACGTGTACCGCAG
CCACGTGGCAGGCCAGATGCTGCATGGGGGCGGCAGCAGGCTCAACAGCGGCAACCGCTG
GTTTGACAAGACGCTGCAGTTCATCGTGGCAGAAGATGGCTCCTGTGGGCTTGTGTACGA
GCATGCTGCAGCNGAGGGTTTCCCTATTGTCACCCTTCTGGACTATGTCATCGAGTACAC
GAAGAAACCCGAGCTTGTGCNGTCTCCCATGGTGCCCCTGCCCATGCCCAAGAAGCTGCG
GTTCAACATCACCCCCGAGATCAAGAGCGACATCGAGAAGGCCAAGCAGAACCTCAGCAT
CATGATCCANNACCTGGATATCACCGTGATGGTGTTCCACCATTTTGGAAAAGACTTCCC
CAAGTCGGAGAAGCTAAGCCCAGATGCCTTCATCCAGATGGCTTTGCAGCTGGCCTACTA
CAGGATCTACGGACAGGCATGTGCCACCTATGAAAGTNCNTCCCTGCGCATGTTTCACCT
GGGCCGCACCGACACCATCCGCTCGGCTTCCATGGACTCACTCACCTTTGTCAAGGCCAT
GGATGACTCCAGCGTCACGGAGCACCAGAAGGTGGAGCTGCTGCGGAAGGCCGTGCAGGC
CCACCGGGGCTACACCGACCGGGCCATCCGCGGGGAGGCCTTTGGTCGACACCTGCTGGG
CCTGAAGCTGCAGGCCATCGAGGACCTGGTGAGCACGCCCGACATCTTCATGGACACCTC
CTACGCCATCGCCATGCACTTCCACCTCTCCACCAGCCAGGTCCCTGCCAAGACAGACTG
TGTCATGTTCTTCGGGCCCGTGGTCCCCGACGGCTACGGTGTCTGCTATAACCCCATGGA
GGCCCACATCAACTTCTCCCTGTCGGCCTACAACAGCTGCGCGGAGACCAACGCCGCCCG
CCTGGCGCATTACCTGGAGAAGGCGCTCCTGGACATGCGTGCCCTGCTGCAGAGCCACCC
CCGGGCCAAGCTCTGA
Enzyme 1 GenBank Gene ID X78706 Link Image
Enzyme 1 GeneCard ID CRAT Link Image
Enzyme 1 GenAtlas ID CRAT Link Image
Enzyme 1 HGNC ID HGNC:2342 Link Image
Enzyme 1 Chromosome Location 9
Enzyme 1 Locus 9q34.1
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Corti O, Finocchiaro G, Rossi E, Zuffardi O, DiDonato S: Molecular cloning of cDNAs encoding human carnitine acetyltransferase and mapping of the corresponding gene to chromosome 9q34.1. Genomics. 1994 Sep 1;23(1):94-9. [PubMed Link Image]
  2. Corti O, DiDonato S, Finocchiaro G: Divergent sequences in the 5' region of cDNA suggest alternative splicing as a mechanism for the generation of carnitine acetyltransferases with different subcellular localizations. Biochem J. 1994 Oct 1;303 ( Pt 1):37-41. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5542
Enzyme 2 Name Peroxisomal carnitine O-octanoyltransferase
Enzyme 2 Synonyms
  1. COT
Enzyme 2 Gene Name CROT
Enzyme 2 Protein Sequence >Peroxisomal carnitine O-octanoyltransferase 
MENQLAKSTEERTFQYQDSLPSLPVPSLEESLKKYLESVKPFANQEEYKKTEEIVQKFQS
GIGEKLHQKLLERAKGKRNWLEEWWLNVAYLDVRIPSQLNVNFAGPAAHFEHYWPPKEGT
QLERGSITLWHNLNYWQLLRKEKVPVHKVGNTPLDMNQFRMLFSTCKVPGITRDSIMNYF
RTESEGRSPNHIVVLCRGRAFVFDVIHEGCLVTPPELLRQLTYIHKKCHSEPDGPGIAAL
TSEERTRWAKAREYLIGLDPENLALLEKIQSSLLVYSMEDSSPHVTPEDYSEIIAAILIG
DPTVRWGDKSYNLISFSNGVFGCNCDHAPFDAMIMVNISYYVDEKIFQNEGRWKGSEKVR
DIPLPEELIFIVDEKVLNDINQAKAQYLREASDLQIAAYAFTSFGKKLTKNKMLHPDTFI
QLALQLAYYRLHGHPGCCYETAMTRHFYHGRTETMRSCTVEAVRWCQSMQDPSVNLRERQ
QKMLQAFAKHNKMMKDCSAGKGFDRHLLGLLLIAKEEGLPVPELFTDPLFSKSGGGGNFV
LSTSLVGYLRVQGVVVPMVHNGYGFFYHIRDDRFVVACSAWKSCPETDAEKLVQLTFCAF
HDMIQLMNSTHL
Enzyme 2 Number of Residues 612
Enzyme 2 Molecular Weight 70179
Enzyme 2 Theoretical pI 7.09
Enzyme 2 GO Classification
Function
  • acyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring groups other than amino-acyl groups
Process
—
Component
—
Enzyme 2 General Function Not Available
Enzyme 2 Specific Function Beta-oxidation of fatty acids. The highest activity concerns the C6 to C10 chain length substrate. Converts the end product of pristanic acid beta oxidation, 4,8-dimethylnonanoyl- CoA, to its corresponding carnitine ester
Enzyme 2 Pathways Not Available
Enzyme 2 Reactions
  • octanoyl-CoA + L-carnitine = CoA + L-octanoylcarnitine
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 6066280 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID Q9UKG9 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name OCTC_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1839 bp 
ATGGAAAATCAATTGGCTAAATCAACTGAAGAACGAACATTTCAGTACCAGGATTCTCTT
CCATCACTGCCTGTTCCTTCACTTGAAGAATCATTAAAAAAATACCTTGAATCAGTGAAA
CCATTTGCAAATCAAGAAGAATATAAGAAAACTGAAGAAATAGTTCAAAAATTTCAAAGT
GGGATTGGAGAAAAATTGCACCAGAAATTGCTTGAAAGAGCAAAAGGAAAAAGAAATTGG
CTGGAAGAGTGGTGGCTGAATGTTGCCTATCTGGATGTTCGTATACCATCACAATTGAAT
GTCAACTTTGCGGGTCCTGCAGCTCATTTTGAACACTACTGGCCTCCAAAGGAAGGGACT
CAATTAGAAAGAGGAAGTATAACTCTTTGGCATAACTTGAACTACTGGCAGCTATTAAGA
AAAGAAAAGTTGCCTGTTCATAAAGTTGGAAATACTCCTCTAGATATGAATCAATTCCGA
ATGCTATTTTCTACCTGCAAGGTTCCAGGAATTACTAGAGACTCCATTATGAATTATTTT
AGGACTGAGAGTGAAGGGCGTTCCCCAAACCACATTGTAGTGCTGTGTCGAGGCCGAGCT
TTTGTCTTTGATGTAATACATGAAGGATGTTTGGTCACCCCGCCAGAGCTTCTCAGACAA
CTGACATATATCCACAAGAAGTGCCATAGTGAACCTGATGGACCTGGGATTGCAGCATTA
ACTAGTGAGGAGCGAACTCGATGGGCTAAGGCACGAGAATATCTGATTGGTCTTGATCCA
GAGAACTTGGCTTTGTTAGAAAAAATTCAGAGTAGTTTACTGGTATATTCCATGGAGGAT
AGCAGTCCACATGTAACACCAGAGGATTATTCTGAGATTATTGCAGCCATCCTTATTGGA
GATCCAACAGTACGCTGGGGTGACAAATCCTATAACTTGATTTCCTTTTCTAATGGAGTA
TTTGGCTGTAATTGTGATCATGCTCCTTTTGATGCAATGATTATGGTGAACATCAGTTAT
TATGTGGATGAGAAAATTTTTCAGAATGAAGGAAGATGGAAGGGTTCAGAGAAGGTACGA
GATATACCACTTCCAGAAGAGCTCATTTTCATTGTGGATGAGAAAGTTTTAAATGACATC
AACCAAGCTAAAGCCCAGTATCTCAGGGAGGCATCTGATCTACAGATTGCGGCTTATGCC
TTTACATCTTTTGGCAAAAAGCTAACCAAGAACAAGATGCTTCACCCGGATACGTTTATT
CAGCTTGCACTTCAGCTGGCCTATTACAGACTTCATGGACACCCTGGTTGTTGCTATGAA
ACAGCTATGACAAGACATTTTTATCATGGCCGTACAGAGACTATGCGATCATGCACAGTT
GAAGCAGTGAGGTGGTGCCAGTCCATGCAGGATCCTTCTGTCAATCTTCGTGAGCGGCAG
CAAAAGATGTTACAAGCTTTTGCAAAGCATAATAAAATGATGAAAGATTGTTCAGCTGGA
AAAGGATTTGATCGTCACCTTTTAGGTCTCTTACTCATAGCAAAAGAGGAAGGTCTTCCT
GTTCCAGAACTCTTTACGGACCCACTTTTTTCCAAAAGCGGAGGAGGTGGAAATTTTGTT
CTCTCAACAAGTCTGGTTGGCTATTTACGAGTCCAGGGAGTGGTAGTTCCCATGGTACAC
AATGGTTATGGATTTTTCTACCATATCAGAGATGACAGGTTTGTTGTGGCCTGTTCAGCC
TGGAAATCCTGTCCCGAGACTGATGCGGAAAAGCTAGTTCAGCTGACTTTTTGTGCTTTT
CATGATATGATACAGCTGATGAACTCTACTCATCTTTAG
Enzyme 2 GenBank Gene ID AF168793 Link Image
Enzyme 2 GeneCard ID CROT Link Image
Enzyme 2 GenAtlas ID CROT Link Image
Enzyme 2 HGNC ID HGNC:2366 Link Image
Enzyme 2 Chromosome Location 7
Enzyme 2 Locus 7q21.1
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Ferdinandusse S, Mulders J, IJlst L, Denis S, Dacremont G, Waterham HR, Wanders RJ: Molecular cloning and expression of human carnitine octanoyltransferase: evidence for its role in the peroxisomal beta-oxidation of branched-chain fatty acids. Biochem Biophys Res Commun. 1999 Sep 16;263(1):213-8. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5543
Enzyme 3 Name Carnitine O-palmitoyltransferase I, muscle isoform
Enzyme 3 Synonyms
  1. CPT I
  2. CPTI-M
  3. Carnitine palmitoyltransferase 1B
  4. Carnitine palmitoyltransferase I-like protein
Enzyme 3 Gene Name CPT1B
Enzyme 3 Protein Sequence >Carnitine O-palmitoyltransferase I, muscle isoform 
MAEAHQAVAFQFTVTPDGVDFRLSREALKHVYLSGINSWKKRLIRIKNGILRGVYPGSPT
SWLVVIMATVGSSFCNVDISLGLVSCIQRCLPQGCGPYQTPQTRALLSMAIFSTGVWVTG
IFFFRQTLKLLLCYHGWMFEMHGKTSNLTRIWAMCIRLLSSRHPMLYSFQTSLPKLPVPR
VSATIQRYLESVRPLLDDEEYYRMELLAKEFQDKTAPRLQKYLVLKSWWASNYVSDWWEE
YIYLRGRSPLMVNSNYYVMDLVLIKNTDVQAARLGNIIHAMIMYRRKLDREEIKPVMALG
IVPMCSYQMERMFNTTRIPGKDTDVLQHLSDSRHVAVYHKGRFFKLWLYEGARLLKPQDL
EMQFQRILDDPSPPQPGEEKLAALTAGGRVEWAQARQAFFSSGKNKAALEAIERAAFFVA
LDEESYSYDPEDEASLSLYGKALLHGNCYNRWFDKSFTLISFKNGQLGLNAEHAWADAPI
IGHLWEFVLGTDSFHLGYTETGHCLGKPNPALAPPTRLQWDIPKQCQAVIESSYQVAKAL
ADDVELYCFQFLPFGKGLIKKCRTSPDAFVQIALQLAHFRDRGKFCLTYEASMTRMFREG
RTETVRSCTSESTAFVQAMMEGSHTKADLRDLFQKAAKKHQNMYRLAMTGAGIDRHLFCL
YLVSKYLGVSSPFLAEVLSEPWRLSTSQIPQSQIRMFDPEQHPNHLGAGGGFGPVADDGY
GVSYMIAGENTIFFHISSKFSSSETNAQRFGNHIRKALLDIADLFQVPKAYS
Enzyme 3 Number of Residues 772
Enzyme 3 Molecular Weight 87802
Enzyme 3 Theoretical pI 8.77
Enzyme 3 GO Classification
Function
  • acyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring groups other than amino-acyl groups
Process
—
Component
—
Enzyme 3 General Function Not Available
Enzyme 3 Specific Function Palmitoyl-CoA + L-carnitine = CoA + L- palmitoylcarnitine
Enzyme 3 Pathways
Enzyme 3 Reactions
  • palmitoyl-CoA + L-carnitine = CoA + L-palmitoylcarnitine
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • 48-73 103-122
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 1621202 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID Q92523 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name CPT1B_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >2319 bp 
ATGGCGGAAGCTCACCAGGCCGTGGCCTTCCAGTTCACGGTGACCCCAGACGGGGTCGAC
TTCCGGCTCAGTCGGGAGGCCCTGAAACACGTCTACCTGTCTGGGATCAACTCCTGGAAG
AAACGCCTGATCCGCATCAAGAATGGCATCCTCAGGGGCGTGTACCCTGGCAGCCCCACC
AGCTGGCTGGTCGTCATCATGGCAACAGTGGGTTCCTCCTTCTGCAACGTGGACATCTCC
TTGGGGCTGGTCAGTTGCATCCAGAGATGCCTCCCTCAGGGGTGTGGCCCCTACCAGACC
CCGCAGACCCGGGCACTTCTCAGCATGGCCATCTTCTCCACGGGCGTCTGGGTGACGGGC
ATCTTCTTCTTCCGCCAAACCCTGAAGCTGCTTCTCTGCTACCATGGGTGGATGTTTGAG
ATGCATGGCAAGACCAGCAACTTGACCAGGATCTGGGCTATGTGTATCCGCCTTCTATCC
AGCCGGCACCCTATGCTCTACAGCTTCCAGACATCTCTGCCCAAGCTTCCTGTGCCCAGG
GTGTCAGCCACAATTCAGCGGTACCTAGAGTCTGTGCGCCCCTTGTTGGATGATGAGGAA
TATTACCGCATGGAGTTGCTGGCCAAAGAATTCCAGGACAAGACTGCCCCCAGGCTGCAG
AAATACCTGGTGCTCAAGTCATGGTGGGCAAGTAACTATGTGAGTGACTGGTGGGAAGAG
TACATCTACCTTCGAGGCAGGAGCCCTCTCATGGTGAACAGCAACTATTATGTCATGGAC
CTTGTGCTCATCAAGAATACAGACGTGCAGGCAGCCCGCCTGGGAAACATCATCCACGCC
ATGATCATGTATCGCCGTAAACTGGACCGTGAAGAAATCAAGCCTGTGATGGCACTGGGC
ATAGTGCCTATGTGCTCCTACCAGATGGAGAGGATGTTCAACACCACTCGGATCCCGGGC
AAGGACACAGATGTGCTACAGCACCTCTCAGACAGCCGGCACGTGGCTGTCTACCACAAG
GGACGCTTCTTCAAGCTGTGGCTCTATGAGGGCGCCCGTCTGCTCAAGCCTCAGGATCTG
GAGATGCAGTTCCAGAGGATCCTGGACGACCCCTCCCCACCTCAGCCTGGGGAGGAGAAG
CTGGCAGCCCTCACTGCAGGAGGAAGGGTGGAGTGGGCGCAGGCACGCCAGGCCTTCTTT
AGCTCTGGAAAGAATAAGGCTGCCTTGGAGGCCATCGAGCGTGCCGCTTTCTTCGTGGCC
CTGGATGAGGAATCCTACTCCTATGACCCCGAAGATGAGGCCAGCCTCAGCCTCTATGGC
AAGGCCCTGCTACATGGCAACTGCTACAACAGGTGGTTTGACAAATCCTTCACTCTCATT
TCCTTCAAGAATGGCCAGTTGGGTCTCAATGCAGAGCATGCGTGGGCAGATGCTCCCATC
ATTGGGCACCTCTGGGAGTTTGTCCTGGGCACAGACAGCTTCCACCTGGGCTACACGGAG
ACCGGGCACTGCCTGGGCAAACCGAACCCTGCGCTCGCACCTCCTACACGGCTGCAGTGG
GACATTCCAAAACAGTGCCAGGCGGTCATCGAGAGTTCCTACCAGGTGGCCAAGGCGTTG
GCAGACGACGTGGAGTTGTACTGCTTCCAGTTCCTGCCCTTTGGCAAAGGCCTCATCAAG
AAGTGCCGGACCAGCCCTGATGCCTTTGTGCAGATCGCGCTGCAGCTGGCTCACTTCCGG
GACAGGGGTAAGTTCTGCCTGACCTATGAGGCCTCAATGACCAGAATGTTCCGGGAGGGA
CGGACTGAGACTGTGCGTTCCTGTACCAGCGAGTCCACAGCCTTTGTGCAGGCCATGATG
GAGGGGTCCCACACAAAAGCAGACCTGCGAGATCTCTTCCAGAAGGCTGCTAAGAAGCAC
CAGAATATGTACCGCCTGGCCATGACCGGGGCAGGGATCGACAGGCACCTCTTCTGCCTT
TACTTGGTCTCCAAGTACCTAGGAGTCAGCTCTCCTTTCCTTGCTGAGGTGCTCTCGGAA
CCCTGGCGTCTCTCCACCAGCCAGATCCCCCAATCCCAGATCCGCATGTTCGACCCAGAG
CAGCACCCCAATCACCTGGGCGCTGGAGGTGGCTTTGGCCCTGTAGCAGATGATGGCTAT
GGAGTTTCCTACATGATTGCAGGCGAGAACACGATCTTCTTCCACATCTCCAGCAAGTTC
TCAAGCTCAGAGACGAACGCCCAGCGCTTTGGAAACCACATCCGCAAAGCCCTGCTGGAC
ATTGCTGATCTTTTCCAAGTTCCCAAGGCCTACAGCTGA
Enzyme 3 GenBank Gene ID D87812 Link Image
Enzyme 3 GeneCard ID CPT1B Link Image
Enzyme 3 GenAtlas ID CPT1B Link Image
Enzyme 3 HGNC ID HGNC:2329 Link Image
Enzyme 3 Chromosome Location 22
Enzyme 3 Locus 22q13.33
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Yamazaki N, Shinohara Y, Shima A, Yamanaka Y, Terada H: Isolation and characterization of cDNA and genomic clones encoding human muscle type carnitine palmitoyltransferase I. Biochim Biophys Acta. 1996 Jun 7;1307(2):157-61. [PubMed Link Image]
  2. Zhu H, Shi J, de Vries Y, Arvidson DN, Cregg JM, Woldegiorgis G: Functional studies of yeast-expressed human heart muscle carnitine palmitoyltransferase I. Arch Biochem Biophys. 1997 Nov 1;347(1):53-61. [PubMed Link Image]
  3. Britton CH, Mackey DW, Esser V, Foster DW, Burns DK, Yarnall DP, Froguel P, McGarry JD: Fine chromosome mapping of the genes for human liver and muscle carnitine palmitoyltransferase I (CPT1A and CPT1B). Genomics. 1997 Feb 15;40(1):209-11. [PubMed Link Image]
  4. van der Leij FR, Takens J, van der Veen AY, Terpstra P, Kuipers JR: Localization and intron usage analysis of the human CPT1B gene for muscle type carnitine palmitoyltransferase I. Biochim Biophys Acta. 1997 May 30;1352(2):123-8. [PubMed Link Image]
  5. Yamazaki N, Yamanaka Y, Hashimoto Y, Shinohara Y, Shima A, Terada H: Structural features of the gene encoding human muscle type carnitine palmitoyltransferase I. FEBS Lett. 1997 Jun 16;409(3):401-6. [PubMed Link Image]
  6. Hirosawa M, Nagase T, Murahashi Y, Kikuno R, Ohara O: Identification of novel transcribed sequences on human chromosome 22 by expressed sequence tag mapping. DNA Res. 2001 Feb 28;8(1):1-9. [PubMed Link Image]
  7. Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 5544
Enzyme 4 Name Carnitine O-palmitoyltransferase I, liver isoform
Enzyme 4 Synonyms
  1. CPT I
  2. CPTI-L
  3. Carnitine palmitoyltransferase 1A
Enzyme 4 Gene Name CPT1A
Enzyme 4 Protein Sequence >Carnitine O-palmitoyltransferase I, liver isoform 
MAEAHQAVAFQFTVTPDGIDLRLSHEALRQIYLSGLHSWKKKFIRFKNGIITGVYPASPS
SWLIVVVGVMTTMYAKIDPSLGIIAKINRTLETANCMSSQTKNVVSGVLFGTGLWVALIV
TMRYSLKVLLSYHGWMFTEHGKMSRATKIWMGMVKIFSGRKPMLYSFQTSLPRLPVPAVK
DTVNRYLQSVRPLMKEEDFKRMTALAQDFAVGLGPRLQWYLKLKSWWATNYVSDWWEEYI
YLRGRGPLMVNSNYYAMDLLYILPTHIQAARAGNAIHAILLYRRKLDREEIKPIRLLGST
IPLCSAQWERMFNTSRIPGEETDTIQHMRDSKHIVVYHRGRYFKVWLYHDGRLLKPREME
QQMQRILDNTSEPQPGEARLAALTAGDRVPWARCRQAYFGRGKNKQSLDAVEKAAFFVTL
DETEEGYRSEDPDTSMDSYAKSLLHGRCYDRWFDKSFTFVVFKNGKMGLNAEHSWADAPI
VAHLWEYVMSIDSLQLGYAEDGHCKGDINPNIPYPTRLQWDIPGECQEVIETSLNTANLL
ANDVDFHSFPFVAFGKGIIKKCRTSPDAFVQLALQLAHYKDMGKFCLTYEASMTRLFREG
RTETVRSCTTESCDFVRAMVDPAQTVEQRLKLFKLASEKHQHMYRLAMTGSGIDRHLFCL
YVVSKYLAVESPFLKEVLSEPWRLSTSQTPQQQVELFDLENNPEYVSSGGGFGPVADDGY
GVSYILVGENLINFHISSKFSCPETDSHRFGRHLKEAMTDIITLFGLSSNSKK
Enzyme 4 Number of Residues 773
Enzyme 4 Molecular Weight 88369
Enzyme 4 Theoretical pI 8.84
Enzyme 4 GO Classification
Function
  • acyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring groups other than amino-acyl groups
Process
—
Component
—
Enzyme 4 General Function Not Available
Enzyme 4 Specific Function Palmitoyl-CoA + L-carnitine = CoA + L- palmitoylcarnitine
Enzyme 4 Pathways
Enzyme 4 Reactions
  • palmitoyl-CoA + L-carnitine = CoA + L-palmitoylcarnitine
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • 48-73 103-122
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 755646 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID P50416 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name CPT1A_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >2322 bp 
ATGGCAGAAGCTCACCAAGCTGTGGCCTTTCAGTTCACGGTCACTCCGGACGGGATTGAC
CTGCGGCTGAGCCATGAAGCTCTTAGACAAATCTATCTCTCTGGACTTCATTCCTGGAAA
AAGAAGTTCATCAGATTCAAGAACGGCATCATCACTGGCGTGTACCCGGCAAGCCCCTCC
AGTTGGCTTATCGTGGTGGTGGGCGTGATGACAACGATGTACGCCAAGATCGACCCCTCG
TTAGGAATAATTGCAAAAATCAATCGGACTCTGGAAACGGCCAACTGCATGTCCAGCCAG
ACGAAGAACGTGGTCAGCGGCGTGCTGTTTGGCACCGGCCTGTGGGTGGCCCTCATCGTC
ACCATGCGCTACTCCCTGAAAGTGCTGCTCTCCTACCACGGGTGGATGTTCACTGAGCAC
GGCAAGATGAGTCGTGCCACCAAGATCTGGATGGGTATGGTCAAGATCTTTTCAGGCCGA
AAACCCATGTTGTACAGCTTCCAGACATCGCTGCCTCGCCTGCCGGTCCCGGCTGTCAAA
GACACTGTGAACAGGTATCTACAGTCGGTGAGGCCTCTTATGAAGGAAGAAGACTTCAAA
CGGATGACAGCACTTGCTCAAGATTTTGCTGTCGGTCTTGGACCAAGATTACAGTGGTAT
TTGAAGTTAAAATCCTGGTGGGCTACAAATTACGTGAGCGACTGGTGGGAGGAGTACATC
TACCTCCGAGGACGAGGGCCGCTCATGGTGAACAGCAACTATTATGCCATGGATCTGCTG
TATATCCTTCCAACTCACATTCAGGCAGCAAGAGCCGGCAACGCCATCCATGCCATCCTG
CTTTACAGGCGCAAACTGGACCGGGAGGAAATCAAACCAATTCGTCTTTTGGGATCCACG
ATTCCACTCTGCTCCGCTCAGTGGGAGCGGATGTTTAATACTTCCCGGATCCCAGGAGAG
GAGACAGACACCATCCAGCACATGAGAGACAGCAAGCACATCGTCGTGTACCATCGAGGA
CGCTACTTCAAGGTCTGGCTCTACCATGATGGGCGGCTGCTGAAGCCCCGGGAGATGGAG
CAGCAGATGCAGAGGATCCTGGACAATACCTCGGAGCCTCAGCCCGGGGAGGCCAGGCTG
GCAGCCCTCACCGCAGGAGACAGAGTTCCCTGGGCCAGGTGTCGTCAGGCCTATTTTGGA
CGTGGGAAAAATAAGCAGTCTCTTGATGCTGTGGAGAAAGCAGCGTTCTTCGTGACGTTA
GATGAAACTGAAGAAGGATACAGAAGTGAAGACCCGGATACGTCAATGGACAGCTACGCC
AAATCTCTACTACACGGCCGATGTTACGACAGGTGGTTTGACAAGTCGTTCACGTTTGTT
GTCTTCAAAAACGGGAAGATGGGCCTCAACGCTGAACACTCCTGGGCAGATGCGCAGATC
GTGGCCCACCTTTGGGAGTACGTCATGTCCATTGACAGCCTCCAGCTGGGCTATGCGGAG
GATGGGCACTGCAAAGGCGACATCAATCCGAACATTCCGTACCCCACCAGGCTGCAGTGG
GACATCCCGGGGGAATGTCAAGAGGTTATAGAGACCTCCCTGAACACCGCAAATCTTCTG
GCAAACGACGTGGATTTCCATTCCTTCCCATTCGTAGCCTTTGGTAAAGGAATCATCAAG
AAATGTCGCACGAGCCCAGACACCTTTGTGCAGCTGGCCCTCCAGCTGGCGCACTACAAG
GACATGGGCAAGTTTTGCCTCACATACGAGGCCTCCATGACCCGGCTCTTCCGAGAGGGG
AGGACGGAGACCGTGCGCTCCTGCACCACTGAGTCATGCGACTTCGTGCGGGCCATGGTG
GACCCGGCCCAGACGGTGGAACAGAGGCTGAAGTTGTTCAAGTTGGCGTCTGAGAAGCAT
CAGCATATGTATCGCCTCGCCATGACCGGCTCTGGGATCGATCGTCACCTCTTCTGCCTT
TACGTGGTGTCTAAATATCTCGCTGTGGAGTCCCCTTTCCTTAAGGAAGTTTTATCTGAG
CCTTGGAGATTATCAACAAGCCAGACCCCTCAGCAGCAAGTGGAGCTGTTTGACTTGGAG
AATAACCCAGAGTACGTGTCCAGCGGAGGGGGCTTTGGACCGGTTGCTGATGACGGCTAT
GGTGTGTCGTACATCCTTGTGGGAGAGAACCTCATCAATTTCCACATTTCTTCCAAGTTC
TCTTGCCCTGAGACGGATTCTCATCGCTTTGGAAGGCACCTGAAAGAAGCAATGACTGAC
ATCATCACTTTGTTTGGTCTCAGTTCTAATTCCAAAAAGTAA
Enzyme 4 GenBank Gene ID L39211 Link Image
Enzyme 4 GeneCard ID CPT1A Link Image
Enzyme 4 GenAtlas ID CPT1A Link Image
Enzyme 4 HGNC ID HGNC:2328 Link Image
Enzyme 4 Chromosome Location 11
Enzyme 4 Locus 11q13.1-q13.2
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Britton CH, Schultz RA, Zhang B, Esser V, Foster DW, McGarry JD: Human liver mitochondrial carnitine palmitoyltransferase I: characterization of its cDNA and chromosomal localization and partial analysis of the gene. Proc Natl Acad Sci U S A. 1995 Mar 14;92(6):1984-8. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 5546
Enzyme 5 Name Carnitine O-palmitoyltransferase 2, mitochondrial precursor
Enzyme 5 Synonyms
  1. Carnitine palmitoyltransferase II
  2. CPT II
Enzyme 5 Gene Name CPT2
Enzyme 5 Protein Sequence >Carnitine O-palmitoyltransferase 2, mitochondrial precursor 
MVPRLLLRAWPRGPAVGPGAPSRPLSAGSGPGQYLQRSIVPTMHYQDSLPRLPIPKLEDT
IRRYLSAQKPLLNDGQFRKTEQFCKSFENGIGKELHEQLVALDKQNKHTSYISGPWFDMY
LSARDSVVLNFNPFMAFNPDPKSEYNDQLTRATNMTVSAIRFLKTLRAGLLEPEVFHLNP
AKSDTITFKRLIRFVPSSLSWYGAYLVNAYPLDMSQYFRLFNSTRLPKPSRDELFTDDKA
RHLLVLRKGNFYIFDVLDQDGNIVSPSEIQAHLKYILSDSSPAPEFPLAYLTSENRDIWA
ELRQKLMSSGNEESLRKVDSAVFCLCLDDFPIKDLVHLSHNMLHGDGTNRWFDKSFNLII
AKDGSTAVHFEHSWGDGVAVLRFFNEVFKDSTQTPAVTPQSQPATTDSTVTVQKLNFELT
DALKTGITAAKEKFDATMKTLTIDCVQFQRGGKEFLKKQKLSPDAVAQLAFQMAFLRQYG
QTVATYESCSTAAFKHGRTETIRPASVYTKRCSEAFVREPSRHSAGELQQMMVECSKYHG
QLTKEAAMGQGFDRHLFALRHLAAAKGIILPELYLDPAYGQINHNVLSTSTLSSPAVNLG
GFAPVVSDGFGVGYAVHDNWIGCNVSSYPGRNAREFLQCVEKALEDMFDALEGKSIKS
Enzyme 5 Number of Residues 658
Enzyme 5 Molecular Weight 73778
Enzyme 5 Theoretical pI 8.30
Enzyme 5 GO Classification
Function
  • acyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring groups other than amino-acyl groups
Process
—
Component
—
Enzyme 5 General Function Not Available
Enzyme 5 Specific Function Palmitoyl-CoA + L-carnitine = CoA + L- palmitoylcarnitine
Enzyme 5 Pathways
Enzyme 5 Reactions
  • palmitoyl-CoA + L-carnitine = CoA + L-palmitoylcarnitine
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • 1-15
Enzyme 5 Transmembrane Regions Not Available
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 1041195 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID P23786 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name CPT2_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >1977 bp 
ATGGTGCCCCGCCTGCTGCTGCGCGCCTGGCCCCGGGGCCCCGCGGTTGGTCCGGGAGCC
CCCAGTCGGCCCCTCAGCGCCGGCTCCGGGCCCGGCCAGTACCTGCAGCGCAGCATCGTG
CCCACCATGCACTACCAGGACAGCCTGCCCAGGCTGCCTATTCCCAAACTTGAAGACACC
ATTAGGAGATACCTCAGTGCACAGAAGCCTCTCTTGAATGATGGCCAGTTCAGGAAAACA
GAACAATTTTGCAAGAGTTTTGAAAATGGGATTGGAAAAGAACTGCATGAGCAGCTGGTT
GCTCTGGACAAACAGAATAAACATACAAGCTACATTTCGGGACCCTGGTTTGATATGTAC
CTATCTGCTCGAGACTCCGTTGTTCTGAACTTTAATCCATTTATGGCTTTCAATCCTGAC
CCAAAATCTGAGTATAATGACCAGCTCACCCGGGCAACCAACATGACTGTTTCTGCCATC
CGGTTTCTGAAGACACTCCGGGCTGGCCTTCTGGAGCCAGAAGTGTTCCACTTGAACCCT
GCAAAAAGTGACACTATCACCTTCAAGAGACTCATACGCTTTGTGCCTTCCTCTCTGTCC
TGGTATGGGGCCTACCTGGTCAATGCGTATCCCCTGGATATGTCCCAGTATTTTCGGCTT
TTCAACTCAACTCGTTTACCCAAACCCAGTCGGGATGAACTCTTCACTGATGACAAGGCC
AGACACCTCCTGGTCCTAAGGAAAGGAAATTTTTATATCTTTGATGTCCTGGATCAAGAT
GGGAACATTGTGAGCCCCTCGGAAATCCAGGCACATCTGAAGTACATTCTCTCAGACAGC
AGCCCCGCCCCCGAGTTTCCCCTGGCATACCTGACCAGTGAGAACCGAGACATCTGGGCA
GAGCTCAGGCAGAAGCTGATGAGTAGTGGCAATGAGGAGAGCCTGAGGAAAGTGGACTCG
GCAGTGTTCTGTCTCTGCCTAGATGACTTCCCCATTAAGGACCTTGTCCACTTGTCCCAC
AATATGCTGCATGGGGATGGCACAAACCGCTGGTTTGATAAATCCTTTAACCTCATTATC
GCCAAGGATGGCTCTACTGCCGTCCACTTTGAGCACTCTTGGGGTGATGGTGTGGCAGTG
CTCAGATTTTTTAATGAAGTATTTAAAGACAGCACTCAGACCCCTGCCGTCACTCCACAG
AGCCAGCCAGCTACCACTGACTCTACTGTCACGGTGCAGAAACTCAACTTCGAGCTGACT
GATGCCTTAAAGACTGGCATCACAGCTGCTAAGGAAAAGTTTGATGCCACCATGAAAACC
CTCACTATTGACTGCGTCCAGTTTCAGAGAGGAGGCAAAGAATTCCTGAAGAAGCAAAAG
CTGAGCCCTGACGCAGTTGCCCAGCTGGCATTCCAGATGGCCTTCCTGCGGCAGTACGGG
CAGACAGTGGCCACCTACGAGTCCTGTAGCACTGCCGCATTCAAGCACGGCCGCACTGAG
ACCATCCGCCCGGCCTCCGTCTATACAAAGAGGTGCTCTGAGGCCTTTGTCAGGGAGCCC
TCCAGGCACAGTGCTGGTGAGCTTCAGCAGATGATGGTTGAGTGCTCCAAGTACCATGGC
CAGCTGACCAAAGAAGCAGCAATGGGCCAGGGCTTTGACCGACACTTGTTTGCTCTGCGG
CATCTGGCAGCAGCCAAAGGGATCATCTTGCCTGAGCTCTACCTGGACCCTGCATACGGG
CAGATAAACCACAATGTCCTGTCCACGAGCACACTGAGCAGCCCAGCAGTGAACCTTGGG
GGCTTTGCCCCTGTGGTCTCTGATGGCTTTGGTGTTGGGTATGCTGTTCATGACAACTGG
ATAGGCTGCAATGTCTCTTCCTACCCAGGCCGCAATGCCCGGGAGTTTCTCCAATGTGTG
GAGAAGGCCTTAGAAGACATGTTTGATGCCTTAGAAGGCAAATCCATCAAAAGTTAA
Enzyme 5 GenBank Gene ID U09648 Link Image
Enzyme 5 GeneCard ID CPT2 Link Image
Enzyme 5 GenAtlas ID CPT2 Link Image
Enzyme 5 HGNC ID HGNC:2330 Link Image
Enzyme 5 Chromosome Location 1
Enzyme 5 Locus 1p32
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Finocchiaro G, Taroni F, Rocchi M, Martin AL, Colombo I, Tarelli GT, DiDonato S: cDNA cloning, sequence analysis, and chromosomal localization of the gene for human carnitine palmitoyltransferase. Proc Natl Acad Sci U S A. 1991 Jan 15;88(2):661-5. [PubMed Link Image]
  2. Finocchiaro G, Taroni F, Rocchi M, Liras Martin A, Colombo I, Tarelli GT, DiDonato S: cDNA cloning, sequence analysis, and chromosomal localization of human carnitine palmitoyltransferase. Proc Natl Acad Sci U S A. 1991 Dec 1;88(23):10981. [PubMed Link Image]
  3. Verderio E, Cavadini P, Montermini L, Wang H, Lamantea E, Finocchiaro G, DiDonato S, Gellera C, Taroni F: Carnitine palmitoyltransferase II deficiency: structure of the gene and characterization of two novel disease-causing mutations. Hum Mol Genet. 1995 Jan;4(1):19-29. [PubMed Link Image]
  4. Finocchiaro G, Colombo I, DiDonato S: Purification, characterization and partial amino acid sequences of carnitine palmitoyl-transferase from human liver. FEBS Lett. 1990 Nov 12;274(1-2):163-6. [PubMed Link Image]
  5. Taroni F, Verderio E, Fiorucci S, Cavadini P, Finocchiaro G, Uziel G, Lamantea E, Gellera C, DiDonato S: Molecular characterization of inherited carnitine palmitoyltransferase II deficiency. Proc Natl Acad Sci U S A. 1992 Sep 15;89(18):8429-33. [PubMed Link Image]
  6. Taroni F, Verderio E, Dworzak F, Willems PJ, Cavadini P, DiDonato S: Identification of a common mutation in the carnitine palmitoyltransferase II gene in familial recurrent myoglobinuria patients. Nat Genet. 1993 Jul;4(3):314-20. [PubMed Link Image]
  7. Bonnefont JP, Taroni F, Cavadini P, Cepanec C, Brivet M, Saudubray JM, Leroux JP, Demaugre F: Molecular analysis of carnitine palmitoyltransferase II deficiency with hepatocardiomuscular expression. Am J Hum Genet. 1996 May;58(5):971-8. [PubMed Link Image]
  8. Wataya K, Akanuma J, Cavadini P, Aoki Y, Kure S, Invernizzi F, Yoshida I, Kira J, Taroni F, Matsubara Y, Narisawa K: Two CPT2 mutations in three Japanese patients with carnitine palmitoyltransferase II deficiency: functional analysis and association with polymorphic haplotypes and two clinical phenotypes. Hum Mutat. 1998;11(5):377-86. [PubMed Link Image]
  9. Taggart RT, Smail D, Apolito C, Vladutiu GD: Novel mutations associated with carnitine palmitoyltransferase II deficiency. Hum Mutat. 1999;13(3):210-20. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 5547
Enzyme 6 Name Carnitine O-palmitoyltransferase I, brain isoform
Enzyme 6 Synonyms
  1. Carnitine palmitoyltransferase 1C
  2. CPT IC
Enzyme 6 Gene Name CPT1C
Enzyme 6 Protein Sequence >Carnitine O-palmitoyltransferase I, brain isoform 
MAEAHQAVGFRPSLTSDGAEVELSAPVLQEIYLSGLRSWKRHLSRFWNDFLTGVFPASPL
SWLFLFSAIQLAWFLQLDPSLGLMEKIKELLPDWGGQHHGLRGVLAAALFASCLWGALIF
TLHVALRLLLSYHGWLLEPHGAMSSPTKTWLALVRIFSGRHPMLFSYQRSLPRQPVPSVQ
DTVRKYLESVRPILSDEDFDWTAVLAQEFLRLQASLLQWYLRLKSWWASNYVSDWWEEFV
YLRSRNPLMVNSNYYMMDFLYVTPTPLQAARAGNAVHALLLYRHRLNRQEIPPTLLMGMR
PLCSAQYEKIFNTTRIPGVQKDYIRHLHDSQHVAVFHRGRFFRMGTHSRNSLLSPRALEQ
QFQRILDDPSPACPHEEHLAALTAAPRGTWAQVRTSLKTQAAEALEAVEGAAFFVSLDAE
PAGLTREDPAASLDAYAHALLAGRGHDRWFDKSFTLIVFSNGKLGLSVEHSWADCPISGH
MWEFTLATECFQLGYSTDGHCKGHPDPTLPQPQRLQWDLPDQIHSSISLALRGAKILSEN
VDCHVVPFSLFGKSFIRRCHLSSDSFIQIALQLAHFRDRGQFCLTYESAMTRLFLEGRTE
TVRSCTREACNFVRAMEDKEKTDPQCLALFRVAVDKHQALLKAAMSGQGVDRHLFALYIV
SRFLHLQSPFLTQVHSEQWQLSTSQIPVQQMHLFDVHNYPDYVSSGGGFGPADDHGYGVS
YIFMGDGMITFHISSKKSSTKTDSHRLGQHIEDALLDVASLFQAGQHFKRRFRGSGKENS
RHRCGFLSRQTGASKASMTSTDF
Enzyme 6 Number of Residues 803
Enzyme 6 Molecular Weight 90990
Enzyme 6 Theoretical pI 8.18
Enzyme 6 GO Classification
Function
  • acyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring groups other than amino-acyl groups
Process
—
Component
—
Enzyme 6 General Function Not Available
Enzyme 6 Specific Function Palmitoyl-CoA + L-carnitine = CoA + L- palmitoylcarnitine
Enzyme 6 Pathways
Enzyme 6 Reactions
  • palmitoyl-CoA + L-carnitine = CoA + L-palmitoylcarnitine
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • 53-75 104-126
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 19850304 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID Q8TCG5 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name CPT1C_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >114 bp 
ATGCAAGCGGGAGATTTGGGGCCGGCGCTCAAAATCGGGGGGCGGGGGTGGACTCGGGTT
TGGACCCCAGGATCCGATCAGCGGACCCTTGATTCAACGTGGGCTCCAGCGTGA
Enzyme 6 GenBank Gene ID AF357970 Link Image
Enzyme 6 GeneCard ID CPT1C Link Image
Enzyme 6 GenAtlas ID CPT1C Link Image
Enzyme 6 HGNC ID HGNC:18540 Link Image
Enzyme 6 Chromosome Location 19
Enzyme 6 Locus 19q13.33
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. Price N, van der Leij F, Jackson V, Corstorphine C, Thomson R, Sorensen A, Zammit V: A novel brain-expressed protein related to carnitine palmitoyltransferase I. Genomics. 2002 Oct;80(4):433-42. [PubMed Link Image]
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 5619
Enzyme 7 Name Gamma-butyrobetaine dioxygenase
Enzyme 7 Synonyms
  1. Gamma-butyrobetaine,2- oxoglutarate dioxygenase
  2. Gamma-butyrobetaine hydroxylase
  3. Gamma- BBH
Enzyme 7 Gene Name BBOX1
Enzyme 7 Protein Sequence >Gamma-butyrobetaine dioxygenase 
MACTIQKAEALDGAHLMQILWYDEEESLYPAVWLRDNCPCSDCYLDSAKARKLLVEALDV
NIGIKGLIFDRKKVYITWPDEHYSEFQADWLKKRCFSKQARAKLQRELFFPECQYWGSEL
QLPTLDFEDVLRYDEHAYKWLSTLKKVGIVRLTGASDKPGEVSKLGKRMGFLYLTFYGHT
WQVQDKIDANNVAYTTGKLSFHTDYPALHHPPGVQLLHCIKQTVTGGDSEIVDGFNVCQK
LKKNNPQAFQILSSTFVDFTDIGVDYCDFSVQSKHKIIELDDKGQVVRINFNNATRDTIF
DVPVERVQPFYAALKEFVDLMNSKESKFTFKMNPGDVITFDNWRLLHGRRSYEAGTEISR
HLEGAYADWDVVMSRLRILRQRVENGN
Enzyme 7 Number of Residues 387
Enzyme 7 Molecular Weight 44715
Enzyme 7 Theoretical pI 6.73
Enzyme 7 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
Process
  • cellular metabolism
  • electron transport
  • generation of precursor metabolites and energy
  • metabolism
  • physiological process
Component
—
Enzyme 7 General Function Not Available
Enzyme 7 Specific Function Catalyzes the formation of L-carnitine from gamma- butyrobetaine
Enzyme 7 Pathways
Enzyme 7 Reactions
  • 4-trimethylammoniobutanoate + 2-oxoglutarate + O2 = 3-hydroxy-4-trimethylammoniobutanoate + succinate + CO2
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • None
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 3746805 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID O75936 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name BODG_HUMAN Link Image
Enzyme 7 PDB ID Not Available
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >1164 bp 
ATGGCTTGTACCATCCAAAAGGCAGAAGCACTTGACGGGGCTCATTTGATGCAGATCCTC
TGGTATGATGAGGAAGAGTCTCTCTACCCAGCTGTATGGTTGAGAGACAACTGTCCGTGC
TCTGATTGCTACCTGGATTCTGCAAAAGCACGGAAACTTCTAGTGGAAGCTCTTGATGTG
AACATTGGAATTAAAGGCTTGATATTTGACAGAAAAAAGGTGTACATCACATGGCCCGAT
GAGCATTACAGTGAATTCCAGGCTGATTGGCTGAAGAAAAGATGCTTTTCCAAGCAGGCC
AGAGCAAAGCTCCAAAGAGAATTGTTTTTTCCAGAATGCCAATACTGGGGCTCAGAGCTC
CAGCTACCCACTTTGGATTTTGAAGATGTTTTAAGATATGATGAACATGCATACAAGTGG
CTCTCCACCCTCAAGAAAGTAGGCATAGTAAGACTCACCGGAGCATCTGACAAACCAGGA
GAAGTTTCAAAACTTGGGAAAAGGATGGGTTTCCTCTATCTCACATTTTATGGACATACT
TGGCAAGTGCAAGACAAAATCGATGCAAACAATGTGGCTTACACAACTGGGAAGCTAAGC
TTTCACACTGATTATCCAGCCCTCCATCATCCACCTGGGGTTCAGCTTCTTCACTGCATA
AAGCAAACAGTCACAGGGGGTGATTCAGAAATTGTAGATGGGTTTAATGTGTGCCAAAAA
CTAAAGAAAAATAATCCTCAGGCATTCCAGATTTTGTCCTCTACCTTTGTGGACTTTACA
GACATTGGAGTGGATTACTGTGATTTTTCTGTACAATCAAAACATAAAATTATAGAGTTA
GATGATAAAGGCCAAGTGGTTCGCATCAACTTCAATAACGCAACTAGGGACACAATATTT
GATGTACCTGTTGAAAGAGTTCAGCCTTTTTATGCTGCTCTGAAGGAGTTTGTTGACCTC
ATGAACAGCAAAGAATCCAAGTTTACCTTCAAGATGAATCCAGGTGATGTGATTACTTTT
GATAACTGGCGCTTACTTCATGGCCGACGTAGCTATGAAGCAGGAACTGAGATATCCCGC
CATCTAGAAGGAGCTTATGCTGACTGGGATGTGGTCATGTCAAGGCTTCGTATCTTAAGG
CAGAGGGTGGAGAATGGAAACTGA
Enzyme 7 GenBank Gene ID AF082868 Link Image
Enzyme 7 GeneCard ID BBOX1 Link Image
Enzyme 7 GenAtlas ID BBOX1 Link Image
Enzyme 7 HGNC ID HGNC:964 Link Image
Enzyme 7 Chromosome Location 11
Enzyme 7 Locus 11p14.2
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References
  1. Vaz FM, van Gool S, Ofman R, Ijlst L, Wanders RJ: Carnitine biosynthesis: identification of the cDNA encoding human gamma-butyrobetaine hydroxylase. Biochem Biophys Res Commun. 1998 Sep 18;250(2):506-10. [PubMed Link Image]
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 6935
Enzyme 8 Name Organic cation/carnitine transporter 2
Enzyme 8 Synonyms
  1. Solute carrier family 22 member 5
  2. High-affinity sodium-dependent carnitine cotransporter
Enzyme 8 Gene Name SLC22A5
Enzyme 8 Protein Sequence >Organic cation/carnitine transporter 2 
MRDYDEVTAFLGEWGPFQRLIFFLLSASIIPNGFTGLSSVFLIATPEHRCRVPDAANLSS
AWRNHTVPLRLRDGREVPHSCRRYRLATIANFSALGLEPGRDVDLGQLEQESCLDGWEFS
QDVYLSTIVTEWNLVCEDDWKAPLTISLFFVGVLLGSFISGQLSDRFGRKNVLFVTMGMQ
TGFSFLQIFSKNFEMFVVLFVLVGMGQISNYVAAFVLGTEILGKSVRIIFSTLGVCIFYA
FGYMVLPLFAYFIRDWRMLLVALTMPGVLCVALWWFIPESPRWLISQGRFEEAEVIIRKA
AKANGIVVPSTIFDPSELQDLSSKKQQSHNILDLLRTWNIRMVTIMSIMLWMTISVGYFG
LSLDTPNLHGDIFVNCFLSAMVEVPAYVLAWLLLQYLPRRYSMATALFLGGSVLLFMQLV
PPDLYYLATVLVMVGKFGVTAAFSMVYVYTAELYPTVVRNMGVGVSSTASRLGSILSPYF
VYLGAYDRFLPYILMGSLTILTAILTLFLPESFGTPLPDTIDQMLRVKGMKHRKTPSHTR
MLKDGQERPTILKSTAF
Enzyme 8 Number of Residues 557
Enzyme 8 Molecular Weight 62753
Enzyme 8 Theoretical pI 8.04
Enzyme 8 GO Classification
Function
  • ion transporter activity
  • transporter activity
Process
  • cellular physiological process
  • ion transport
  • physiological process
  • transport
Component
  • cell
  • integral to membrane
  • intrinsic to membrane
  • membrane
Enzyme 8 General Function Carbohydrate transport and metabolism
Enzyme 8 Specific Function Sodium-ion dependent, high affinity carnitine transporter. Involved in the active cellular uptake of carnitine. Transports one sodium ion with one molecule of carnitine. Also transports organic cations such as tetraethylammonium (TEA) without the involvement of sodium. Also Relative uptake activity ratio of carnitine to TEA is 11.3
Enzyme 8 Pathways Not Available
Enzyme 8 Reactions Not Available
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • None
Enzyme 8 Transmembrane Regions
  • 21-41 143-163 173-193 198-218 233-253 258-278 342-362 374-394 407-427 431-451 463-483 489-509
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 3273741 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID O76082 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name S22A5_HUMAN Link Image
Enzyme 8 PDB ID Not Available
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >1674 bp 
ATGCGGGACTACGACGAGGTGACCGCCTTCCTGGGCGAGTGGGGGCCCTTCCAGCGCCTC
ATCTTCTTCCTGCTCAGCGCCAGCATCATCCCCAATGGCTTCACCGGCCTGTCCTCCGTG
TTCCTGATAGCGACCCCGGAGCACCGCTGCCGGGTGCCGGACGCCGCGAACCTGAGCAGC
GCCTGGCGCAACCACACTGTCCCACTGCGGCTGCGGGACGGCCGCGAGGTGCCCCACAGC
TGCCGCCGCTACCGGCTCGCCACCATCGCCAACTTCTCGGCGCTCGGGCTGGAGCCGGGG
CGCGACGTGGACCTGGGGCAGCTGGAGCAGGAGAGCTGTCTGGATGGCTGGGAGTTCAGT
CAGGACGTCTACCTGTCCACCATTGTGACCGAGTGGAACCTGGTGTGTGAGGACGACTGG
AAGGCCCCACTCACAATCTCCTTGTTCTTCGTGGGTGTGCTGTTGGGCTCCTTCATTTCA
GGGCAGCTGTCAGACAGGTTTGGCCGGAAGAATGTGCTGTTCGTGACCATGGGCATGCAG
ACAGGCTTCAGCTTCCTGCAGATCTTCTCGAAGAATTTTGAGATGTTTGTCGTGCTGTTT
GTCCTTGTAGGCATGGGCCAGATCTCCAACTATGTGGCAGCATTTGTCCTGGGGACAGAA
ATTCTTGGCAAGTCAGTTCGTATAATATTCTCTACGTTAGGAGTGTGCATATTTTATGCA
TTTGGCTACATGGTGCTGCCACTGTTTGCTTACTTCATCCGAGACTGGCGGATGCTGCTG
GTGGCGCTGACGATGCCGGGGGTGCTGTGCGTGGCACTCTGGTGGTTCATCCCTGAGTCC
CCCCGATGGCTCATCTCTCAGGGACGATTTGAAGAGGCAGAGGTGATCATCCGCAAGGCT
GCCAAAGCCAATGGGATTGTTGTGCCTTCCACTATCTTTGACCCGAGTGAGTTACAAGAC
CTAAGTTCCAAGAAGCAACAGTCCCACAACATTCTGGATCTGCTTCGAACCTGGAATATC
CGGATGGTCACCATCATGTCCATAATGCTGTGGATGACCATATCAGTGGGCTATTTTGGG
CTTTCGCTTGATACTCCTAACTTGCATGGGGACATCTTTGTGAACTGCTTCCTTTCAGCG
ATGGTTGAAGTCCCAGCATATGTGTTGGCCTGGCTGCTGCTGCAATATTTGCCCCGGCGC
TATTCCATGGCCACTGCCCTCTTCCTGGGTGGCAGTGTCCTTCTCTTCATGCAGCTGGTA
CCCCCAGACTTGTATTATTTGGCTACAGTCCTGGTGATGGTGGGCAAGTTTGGAGTCACG
GCTGCCTTTTCCATGGTCTACGTGTACACAGCCGAGCTGTATCCCACAGTGGTGAGAAAC
ATGGGTGTGGGAGTCAGCTCCACAGCATCCCGCCTGGGCAGCATCCTGTCTCCCTACTTC
GTTTACCTTGGTGCCTACGACCGCTTCCTGCCCTACATTCTCATGGGAAGTCTGACCATC
CTGACAGCCATCCTCACCTTGTTTCTCCCAGAGAGCTTCGGTACCCCACTCCCAGACACC
ATTGACCAGATGCTAAGAGTCAAAGGAATGAAACACAGAAAAACTCCAAGTCACACAAGG
ATGTTAAAAGATGGTCAAGAAAGGCCCACAATCCTTAAAAGCACAGCCTTCTAA
Enzyme 8 GenBank Gene ID AF057164 Link Image
Enzyme 8 GeneCard ID SLC22A5 Link Image
Enzyme 8 GenAtlas ID SLC22A5 Link Image
Enzyme 8 HGNC ID HGNC:10969 Link Image
Enzyme 8 Chromosome Location 5
Enzyme 8 Locus 5q31
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References
  1. Wu X, Prasad PD, Leibach FH, Ganapathy V: cDNA sequence, transport function, and genomic organization of human OCTN2, a new member of the organic cation transporter family. Biochem Biophys Res Commun. 1998 May 29;246(3):589-95. [PubMed Link Image]
  2. Tamai I, Ohashi R, Nezu J, Yabuuchi H, Oku A, Shimane M, Sai Y, Tsuji A: Molecular and functional identification of sodium ion-dependent, high affinity human carnitine transporter OCTN2. J Biol Chem. 1998 Aug 7;273(32):20378-82. [PubMed Link Image]
  3. Nezu J, Tamai I, Oku A, Ohashi R, Yabuuchi H, Hashimoto N, Nikaido H, Sai Y, Koizumi A, Shoji Y, Takada G, Matsuishi T, Yoshino M, Kato H, Ohura T, Tsujimoto G, Hayakawa J, Shimane M, Tsuji A: Primary systemic carnitine deficiency is caused by mutations in a gene encoding sodium ion-dependent carnitine transporter. Nat Genet. 1999 Jan;21(1):91-4. [PubMed Link Image]
  4. Wu X, Huang W, Prasad PD, Seth P, Rajan DP, Leibach FH, Chen J, Conway SJ, Ganapathy V: Functional characteristics and tissue distribution pattern of organic cation transporter 2 (OCTN2), an organic cation/carnitine transporter. J Pharmacol Exp Ther. 1999 Sep;290(3):1482-92. [PubMed Link Image]
  5. Burwinkel B, Kreuder J, Schweitzer S, Vorgerd M, Gempel K, Gerbitz KD, Kilimann MW: Carnitine transporter OCTN2 mutations in systemic primary carnitine deficiency: a novel Arg169Gln mutation and a recurrent Arg282ter mutation associated with an unconventional splicing abnormality. Biochem Biophys Res Commun. 1999 Aug 2;261(2):484-7. [PubMed Link Image]
  6. Vaz FM, Scholte HR, Ruiter J, Hussaarts-Odijk LM, Pereira RR, Schweitzer S, de Klerk JB, Waterham HR, Wanders RJ: Identification of two novel mutations in OCTN2 of three patients with systemic carnitine deficiency. Hum Genet. 1999 Jul-Aug;105(1-2):157-61. [PubMed Link Image]
  7. Tang NL, Ganapathy V, Wu X, Hui J, Seth P, Yuen PM, Wanders RJ, Fok TF, Hjelm NM: Mutations of OCTN2, an organic cation/carnitine transporter, lead to deficient cellular carnitine uptake in primary carnitine deficiency. Hum Mol Genet. 1999 Apr;8(4):655-60. [PubMed Link Image]
  8. Koizumi A, Nozaki J, Ohura T, Kayo T, Wada Y, Nezu J, Ohashi R, Tamai I, Shoji Y, Takada G, Kibira S, Matsuishi T, Tsuji A: Genetic epidemiology of the carnitine transporter OCTN2 gene in a Japanese population and phenotypic characterization in Japanese pedigrees with primary systemic carnitine deficiency. Hum Mol Genet. 1999 Nov;8(12):2247-54. [PubMed Link Image]
  9. Seth P, Wu X, Huang W, Leibach FH, Ganapathy V: Mutations in novel organic cation transporter (OCTN2), an organic cation/carnitine transporter, with differential effects on the organic cation transport function and the carnitine transport function. J Biol Chem. 1999 Nov 19;274(47):33388-92. [PubMed Link Image]
  10. Mayatepek E, Nezu J, Tamai I, Oku A, Katsura M, Shimane M, Tsuji A: Two novel missense mutations of the OCTN2 gene (W283R and V446F) in a patient with primary systemic carnitine deficiency. Hum Mutat. 2000 Jan;15(1):118. [PubMed Link Image]
  11. Wang Y, Kelly MA, Cowan TM, Longo N: A missense mutation in the OCTN2 gene associated with residual carnitine transport activity. Hum Mutat. 2000;15(3):238-45. [PubMed Link Image]
Enzyme 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 7933
Enzyme 9 Name Organic cation/carnitine transporter 1
Enzyme 9 Synonyms
  1. Solute carrier family 22 member 4
  2. Ergothioneine transporter
  3. ET transporter
Enzyme 9 Gene Name SLC22A4
Enzyme 9 Protein Sequence >Organic cation/carnitine transporter 1 
MRDYDEVIAFLGEWGPFQRLIFFLLSASIIPNGFNGMSVVFLAGTPEHRCRVPDAANLSS
AWRNNSVPLRLRDGREVPHSCSRYRLATIANFSALGLEPGRDVDLGQLEQESCLDGWEFS
QDVYLSTVVTEWNLVCEDNWKVPLTTSLFFVGVLLGSFVSGQLSDRFGRKNVLFATMAVQ
TGFSFLQIFSISWEMFTVLFVIVGMGQISNYVVAFILGTEILGKSVRIIFSTLGVCTFFA
VGYMLLPLFAYFIRDWRMLLLALTVPGVLCVPLWWFIPESPRWLISQRRFREAEDIIQKA
AKMNNIAVPAVIFDSVEELNPLKQQKAFILDLFRTRNIAIMTIMSLLLWMLTSVGYFALS
LDAPNLHGDAYLNCFLSALIEIPAYITAWLLLRTLPRRYIIAAVLFWGGGVLLFIQLVPV
DYYFLSIGLVMLGKFGITSAFSMLYVFTAELYPTLVRNMAVGVTSTASRVGSIIAPYFVY
LGAYNRMLPYIVMGSLTVLIGILTLFFPESLGMTLPETLEQMQKVKWFRSGKKTRDSMET
EENPKVLITAF
Enzyme 9 Number of Residues 551
Enzyme 9 Molecular Weight 62156
Enzyme 9 Theoretical pI 7.27
Enzyme 9 GO Classification
Function
  • ion transporter activity
  • transporter activity
Process
  • cellular physiological process
  • ion transport
  • physiological process
  • transport
Component
  • cell
  • integral to membrane
  • intrinsic to membrane
  • membrane
Enzyme 9 General Function Carbohydrate transport and metabolism
Enzyme 9 Specific Function Sodium-ion dependent, low affinity carnitine transporter. Probably transports one sodium ion with one molecule of carnitine. Also transports organic cations such as tetraethylammonium (TEA) without the involvement of sodium. Relative uptake activity ratio of carnitine to TEA is 1.78. A key substrate of this transporter seems to be ergothioneine (ET)
Enzyme 9 Pathways Not Available
Enzyme 9 Reactions Not Available
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • None
Enzyme 9 Transmembrane Regions
  • 21-41 142-162 172-192 198-218 233-253 258-278 338-358 372-392 400-420 427-447 461-481 487-507
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 2605501 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID Q9H015 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name S22A4_HUMAN Link Image
Enzyme 9 PDB ID Not Available
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence >1656 bp 
ATGCGGGACTACGACGAGGTGATCGCCTTCCTGGGCGAGTGGGGGCCCTTCCAGCGCCTC
ATCTTCTTCCTGCTCAGCGCCAGCATCATCCCCAATGGCTTCAATGGTATGTCAGTCGTG
TTCCTGGCGGGGACCCCGGAGCACCGCTGTCGAGTGCCGGACGCCGCGAACCTGAGCAGC
GCCTGGCGCAACAACAGTGTCCCGCTGCGGCTGCGGGACGGCCGCGAGGTGCCCCACAGC
TGCAGCCGCTACCGGCTCGCCACCATCGCCAACTTCTCGGCGCTCGGGCTGGAGCCGGGG
CGCGACGTGGACCTGGGGCAGCTGGAGCAGGAGAGCTGCCTGGATGGCTGGGAGTTCAGC
CAGGACGTCTACCTGTCCACCGTCGTGACCGAGTGGAATCTGGTGTGTGAGGACAACTGG
AAGGTGCCCCTCACCACCTCCCTGTTCTTCGTAGGCGTGCTCCTCGGCTCCTTCGTGTCC
GGGCAGCTGTCAGACAGGTTTGGCAGGAAGAACGTTCTCTTCGCAACCATGGCTGTACAG
ACTGGCTTCAGCTTCCTGCAGATTTTCTCCATCAGCTGGGAGATGTTCACTGTGTTATTT
GTCATCGTGGGCATGGGCCAGATCTCCAACTATGTGGTAGCCTTCATACTAGGAACAGAA
ATTCTTGGCAAGTCAGTTCGTATTATATTCTCTACATTAGGAGTGTGCACATTTTTTGCA
GTTGGCTATATGCTGCTGCCACTGTTTGCTTACTTCATCAGAGACTGGCGGATGCTGCTG
CTGGCGCTGACGGTGCCGGGAGTGCTGTGTGTCCCGCTGTGGTGGTTCATTCCTGAATCT
CCCCGATGGCTGATATCCCAGAGAAGATTTAGAGAGGCTGAAGATATCATCCAAAAAGCT
GCAAAAATGAACAACACAGCTGTACCAGCAGTGATATTTGATTCTGTGGAGGAGCTAAAT
CCCCTGAAGCAGCAGAAAGCTTTCATTCTGGACCTGTTCAGGACTCGGAATATTGCCATA
ATGACCATTATGTCTTTGCTGCTATGGATGCTGACCTCAGTGGGTTACTTTGCTCTGTCT
CTGGATGCTCCTAATTTACATGGAGATGCCTACCTGAACTGTTTCCTCTCTGCCTTGATT
GAAATTCCAGCTTACATTACAGCCTGGCTGCTATTGCGAACGCTGCCCAGGCGTTATATC
ATAGCTGCAGTACTGTTCTGGGGAGGAGGTGTGCTTCTCTTCATTCAACTGGTACCTGTG
GATTATTACTTCTTATCCATTGGTCTGGTCATGCTGGGAAAATTTGGGATCACCTCTGCT
TTCTCCATGCTGTATGTCTTCACTGCTGAGCTCTACCCAACCCTGGTCAGGAACATGGCG
GTGGGGGTCACATCCACGGCCTCCAGAGTGGGCAGCATCATTGCCCCCTACTTTGTTTAC
CTCGGTGCTTACAACAGAATGCTGCCCTACATCGTCATGGGTAGTCTGACTGTCCTGATT
GGAATCTTCACCCTTTTTTTCCCTGAAAGTTTGGGAATGACTCTTCCAGAAACCTTAGAG
CAGATGCAGAAAGTGAAATGGTTCAGATCTGGGAAAAAAACAAGAGACTCAATGGAGACA
GAAGAAAATCCCAAGGTTCTAATAACTGCATTCTGA
Enzyme 9 GenBank Gene ID AB007448 Link Image
Enzyme 9 GeneCard ID SLC22A4 Link Image
Enzyme 9 GenAtlas ID SLC22A4 Link Image
Enzyme 9 HGNC ID HGNC:10968 Link Image
Enzyme 9 Chromosome Location 5
Enzyme 9 Locus 5q31.1
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 General References
  1. Tamai I, Yabuuchi H, Nezu J, Sai Y, Oku A, Shimane M, Tsuji A: Cloning and characterization of a novel human pH-dependent organic cation transporter, OCTN1. FEBS Lett. 1997 Dec 8;419(1):107-11. [PubMed Link Image]
Enzyme 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 8300
Enzyme 10 Name Mitochondrial carnitine/acylcarnitine carrier protein
Enzyme 10 Synonyms
  1. Carnitine/acylcarnitine translocase
  2. CAC
  3. Solute carrier family 25 member 20
Enzyme 10 Gene Name SLC25A20
Enzyme 10 Protein Sequence >Mitochondrial carnitine/acylcarnitine carrier protein 
MADQPKPISPLKNLLAGGFGGVCLVFVGHPLDTVKVRLQTQPPSLPGQPPMYSGTFDCFR
KTLFREGITGLYRGMAAPIIGVTPMFAVCFFGFGLGKKLQQKHPEDVLSYPQLFAAGMLS
GVFTTGIMTPGERIKCLLQIQASSGESKYTGTLDCAKKLYQEFGIRGIYKGTVLTLMRDV
PASGMYFMTYEWLKNIFTPEGKRVSELSAPRILVAGGIAGIFNWAVAIPPDVLKSRFQTA
PPGKYPNGFRDVLRELIRDEGVTSLYKGFNAVMIRAFPANAACFLGFEVAMKFLNWATPN
L
Enzyme 10 Number of Residues 301
Enzyme 10 Molecular Weight 32944
Enzyme 10 Theoretical pI 9.84
Enzyme 10 GO Classification
Function
  • binding
  • transporter activity
Process
  • cellular physiological process
  • physiological process
  • transport
Component
  • cell
  • membrane
  • mitochondrial inner membrane
  • organelle inner membrane
  • organelle membrane
Enzyme 10 General Function Not Available
Enzyme 10 Specific Function Mediates the transport of acylcarnitines of different length across the mitochondrial inner membrane from the cytosol to the mitochondrial matrix for their oxidation by the mitochondrial fatty acid-oxidation pathway
Enzyme 10 Pathways Not Available
Enzyme 10 Reactions Not Available
Enzyme 10 Pfam Domain Function
Enzyme 10 Signals
  • None
Enzyme 10 Transmembrane Regions
  • 13-31 74-93 113-131 171-190 212-230 268-287
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein 2765075 Link Image
Enzyme 10 UniProtKB/Swiss-Prot ID O43772 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name MCAT_HUMAN Link Image
Enzyme 10 PDB ID Not Available
Enzyme 10 Cellular Location Not Available
Enzyme 10 Gene Sequence >906 bp 
ATGGCCGACCAGCCAAAACCCATCAGCCCGCTCAAGAACCTGCTGGCCGGCGGCTTTGGC
GGCGTGTGCCTGGTGTTCGTCGGTCACCCTCTGGACACGGTCAAGGTCCGACTGCAGACA
CAGCCACCGAGTTTGCCTGGACAACCTCCCATGTACTCTGGGACCTTTGACTGTTTCCGG
AAGACTCTTTTTAGAGAGGGCATCACGGGGCTATATCGGGGAATGGCTGCCCCTATCATC
GGGGTCACTCCCATGTTTGCCGTGTGCTTCTTTGGGTTTGGTTTGGGGAAGAAACTACAA
CAGAAACACCCAGAAGATGTGCTCAGCTATCCCCAGCTTTTTGCAGCTGGGATGTTATCT
GGCGTATTCACCACAGGAATCATGACTCCTGGAGAACGGATCAAGTGCTTATTACAGATT
CAGGCTTCTTCAGGAGAAAGCAAGTACACTGGTACCTTGGACTGTGCAAAGAAGCTGTAC
CAGGAGTTTGGGATCCGAGGCATCTACAAAGGGACTGTGCTTACCCTTATGCGAGATGTC
CCAGCTAGTGGAATGTATTTCATGACATATGAATGGCTGAAAAATATCTTCACTCCGGAG
GGAAAGAGGGTCAGTGAGCTCAGTGCCCCTCGGATCTTGGTGGCTGGGGGCATTGCAGGG
ATCTTCAACTGGGCTGTGGCAATCCCCCCAGATGTGCTCAAGTCTCGATTCCAGACTGCA
CCTCCTGGGAAATATCCTAATGGTTTCAGAGATGTGCTGAGGGAGCTGATCCGGGATGAA
GGAGTCACATCCTTGTACAAAGGGTTCAATGCAGTGATGATCCGAGCCTTCCCAGCCAAT
GCGGCCTGTTTCCTTGGCTTTGAAGTTGCCATGAAGTTCCTTAATTGGGCCACCCCCAAC
TTGTGA
Enzyme 10 GenBank Gene ID Y10319 Link Image
Enzyme 10 GeneCard ID SLC25A20 Link Image
Enzyme 10 GenAtlas ID SLC25A20 Link Image
Enzyme 10 HGNC ID HGNC:1421 Link Image
Enzyme 10 Chromosome Location 3
Enzyme 10 Locus 3p21.31
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 General References
  1. Huizing M, Iacobazzi V, Ijlst L, Savelkoul P, Ruitenbeek W, van den Heuvel L, Indiveri C, Smeitink J, Trijbels F, Wanders R, Palmieri F: Cloning of the human carnitine-acylcarnitine carrier cDNA and identification of the molecular defect in a patient. Am J Hum Genet. 1997 Dec;61(6):1239-45. [PubMed Link Image]
  2. Iacobazzi V, Naglieri MA, Stanley CA, Wanders RJ, Palmieri F: The structure and organization of the human carnitine/acylcarnitine translocase (CACT1) gene2. Biochem Biophys Res Commun. 1998 Nov 27;252(3):770-4. [PubMed Link Image]
  3. Al Aqeel AI, Rashid MS, Ruiter JP, Ijlst L, Wanders RJ: A novel molecular defect of the carnitine acylcarnitine translocase gene in a Saudi patient. Clin Genet. 2003 Aug;64(2):163-5. [PubMed Link Image]
Enzyme 10 Metabolite References Not Available
Enzyme 11 [top]
Enzyme 11 ID 8317
Enzyme 11 Name Solute carrier family 22
Enzyme 11 Synonyms
  1. Organic cation transporter, member 16
Enzyme 11 Gene Name SLC22A16
Enzyme 11 Protein Sequence >Solute carrier family 22 
MGSRHFEGIYDHVGHFGRFQRVLYFICAFQNISCGIHYLASVFMGVTPHHVCRPPGNVSQ
VVFHNHSNWSLEDTGALLSSGQKDYVTVQLQNGEIWELSRCSRNKRENTSSLGYEYTGSK
KEFPCVDGYIYDQNTWKSTAVTQWNLVCDRKWLAMLIQPLFMFGVLLGSVTFGYFSDRLG
RRVVLWATSSSMFLFGIAAAFAVDYYTFMAARFFLAMVASGYLVVGFVYVMEFIGMKSRT
WASVHLHSFFAVGTLLVALTGYLVRTWWLYQMILSTVTVPFILCCWVLPETPFWLLSEGR
YEEAQKIVDIMAKWNRASSCKLSELLSLDLQGPVSNSPTEVQKHNLSYLFYNWSITKRTL
TVWLIWFTGSLGFYSFSLNSVNLGGNEYLNLFLLGVVEIPAYTFVCIAMDKVGRRTVLAY
SLFCSALACGVVMVIPQKHYILGVVTAMVGKFAIGAAFGLIYLYTAELYPTIVRSLAVGS
GSMVCRLASILAPFSVDLSSIWIFIPQLFVGTMALLSGVLTLKLPETLGKRLATTWEEAA
KLESENESKSSKLLLTTNNSGLEKTEAITPRDSGLGE
Enzyme 11 Number of Residues 577
Enzyme 11 Molecular Weight 64615
Enzyme 11 Theoretical pI 8.23
Enzyme 11 GO Classification
Function
  • transporter activity
Process
  • cellular physiological process
  • physiological process
  • transport
Component
  • cell
  • integral to membrane
  • intrinsic to membrane
  • membrane
Enzyme 11 General Function Carbohydrate transport and metabolism
Enzyme 11 Specific Function Not Available
Enzyme 11 Pathways Not Available
Enzyme 11 Reactions Not Available
Enzyme 11 Pfam Domain Function
Enzyme 11 Signals
  • 1-35
Enzyme 11 Transmembrane Regions
  • 154-176
  • 183-203
  • 213-235
  • 242-264
  • 274-296
  • 359-378
  • 388-410
  • 417-436
  • 441-463
  • 468-490
  • 500-522
Enzyme 11 Essentiality Not Available
Enzyme 11 GenBank ID Protein 28837286 Link Image
Enzyme 11 UniProtKB/Swiss-Prot ID Q86VW1 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name Q86VW1_HUMAN Link Image
Enzyme 11 PDB ID Not Available
Enzyme 11 Cellular Location Not Available
Enzyme 11 Gene Sequence >1734 bp 
ATGGGGTCCCGCCACTTCGAGGGGATTTATGACCACGTGGGGCACTTCGGCAGATTCCAG
AGAGTCCTCTATTTCATATGTGCCTTCCAGAACATCTCTTGTGGTATTCACTACTTGGCT
TCTGTGTTCATGGGAGTCACCCCTCATCATGTCTGCAGGCCCCCAGGCAATGTGAGTCAG
GTTGTTTTCCATAATCACTCTAATTGGAGTTTGGAGGACACCGGGGCCCTGTTGTCTTCA
GGCCAGAAAGATTATGTTACGGTGCAGTTGCAGAATGGTGAGATCTGGGAGCTCTCAAGG
TGTAGCAGGAATAAGAGGGAGAACACATCGAGTTTGGGCTATGAATACACTGGCAGTAAG
AAAGAGTTTCCTTGTGTGGATGGCTACATATATGACCAGAACACATGGAAAAGCACTGCG
GTGACCCAGTGGAACCTGGTCTGTGACCGAAAATGGCTTGCAATGCTGATCCAGCCCCTA
TTTATGTTTGGAGTCCTACTGGGATCGGTGACTTTTGGCTACTTTTCTGACAGGCTAGGA
CGCCGGGTGGTCTTGTGGGCCACAAGCAGTAGCATGTTTTTGTTTGGAATAGCAGCGGCG
TTTGCAGTTGATTATTACACCTTCATGGCTGCTCGCTTTTTTCTTGCCATGGTTGCAAGT
GGCTATCTTGTGGTGGGGTTTGTCTATGTGATGGAATTCATTGGCATGAAGTCTCGGACA
TGGGCGTCTGTCCATTTGCATTCCTTTTTTGCAGTTGGAACCCTGCTGGTGGCTTTGACA
GGATACTTGGTCAGGACCTGGTGGCTTTACCAGATGATCCTCTCCACAGTGACTGTCCCC
TTTATCCTGTGCTGTTGGGTGCTCCCAGAGACACCTTTTTGGCTTCTCTCAGAGGGACGA
TATGAAGAAGCACAAAAAATAGTTGACATCATGGCCAAGTGGAACAGGGCAAGCTCCTGT
AAACTGTCAGAACTTTTATCACTGGACCTACAAGGTCCTGTTAGTAATAGCCCCACTGAA
GTTCAGAAGCACAACCTATCATATCTGTTTTATAACTGGAGCATTACGAAAAGGACACTT
ACCGTTTGGCTAATCTGGTTCACTGGAAGTTTGGGATTCTACTCGTTTTCCTTGAATTCT
GTTAACTTAGGAGGCAATGAATACTTAAACCTCTTCCTCCTGGGTGTAGTGGAAATTCCC
GCCTACACCTTCGTGTGCATCGCCATGGACAAGGTCGGGAGGAGAACAGTCCTGGCCTAC
TCTCTTTTCTGCAGTGCACTGGCCTGTGGTGTCGTTATGGTGATCCCCCAGAAACATTAT
ATTTTGGGTGTGGTGACAGCTATGGTTGGAAAATTTGCCATCGGGGCAGCATTTGGCCTC
ATTTATCTTTATACAGCTGAGCTGTATCCAACCATTGTAAGATCGCTGGCTGTGGGAAGC
GGCAGCATGGTGTGTCGCCTGGCCAGCATCCTGGCGCCGTTCTCTGTGGACCTCAGCAGC
ATTTGGATCTTCATACCACAGTTGTTTGTTGGGACTATGGCCCTCCTGAGTGGAGTGTTA
ACACTAAAGCTTCCAGAAACCCTTGGGAAACGGCTAGCAACTACTTGGGAGGAGGCTGCA
AAACTGGAGTCAGAGAATGAAAGCAAGTCAAGCAAATTACTTCTCACAACTAATAATAGT
GGGCTGGAAAAAACGGAAGCGATTACCCCCAGGGATTCTGGTCTTGGTGAATAA
Enzyme 11 GenBank Gene ID BC047565 Link Image
Enzyme 11 GeneCard ID SLC22A16 Link Image
Enzyme 11 GenAtlas ID SLC22A16 Link Image
Enzyme 11 HGNC ID HGNC:20302 Link Image
Enzyme 11 Chromosome Location 6
Enzyme 11 Locus 6q22.1|6q21-q22.1
Enzyme 11 SNPs SNPJam Report Link Image
Enzyme 11 General References
  1. Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11. [PubMed Link Image]
Enzyme 11 Metabolite References Not Available
Enzyme 12 [top]
Enzyme 12 ID 15187
Enzyme 12 Name Carnitine O-octanoyltransferase
Enzyme 12 Synonyms Not Available
Enzyme 12 Gene Name CROT
Enzyme 12 Protein Sequence >Carnitine O-octanoyltransferase 
MENQLAKSTEERTFQYQDSLPSLPVPSLEESLKKYLESVKPFANQEEYKKTEEIVQKFQS
GIGEKLHQKLLERAKGKRNWLEEWWLNVAYLDVRIPSQLNVNFAGPAAHFEHYWPPKEGT
QLERGSITLWHNLNYWQLLRKEKVPVHKVGNTPLDMNQFRMLFSTCKVPGITRDSIMNYF
RTESEGRSPNHIVVLCRGRAFVFDVIHEGCLVTPPELLRQLTYIHKKCHSEPDGPGIAAL
TSEERTRWAKAREYLIGLDPENLALLEKIQSSLLVYSMEDSSPHVTPEDYSEIIAAILIG
DPTVRWGDKSYNLISFSNGVFGCNCDHAPFDAMIMVNISYYVDEKIFQNEGRWKGSEKVR
DIPLPEELIFIVDEKVLNDINQAKAQYLREASDLQIAAYAFTSFGKKLTKNKMLHPDTFI
QLALQLAYYRLHGHPGCCYETAMTRHFYHGRTETMRSCTVEAVRWCQSMQDPSVNLRERQ
QKMLQAFAKHNKMMKDCSAGKGFDRHLLGLLLIAKEEGLPVPELFTDPLFSKSGGGGNFV
LSTSLVGYLRVQGVVVPMVHNGYGFFYHIRDDRFVVACSAWKSCPETDAEKLVQLTFCAF
HDMIQLMNSTHL
Enzyme 12 Number of Residues 612
Enzyme 12 Molecular Weight 70179
Enzyme 12 Theoretical pI 7.09
Enzyme 12 GO Classification
Function
  • acyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring groups other than amino-acyl groups
Process
—
Component
—
Enzyme 12 General Function Not Available
Enzyme 12 Specific Function Not Available
Enzyme 12 Pathways Not Available
Enzyme 12 Reactions Not Available
Enzyme 12 Pfam Domain Function
Enzyme 12 Signals
  • None
Enzyme 12 Transmembrane Regions
  • None
Enzyme 12 Essentiality Not Available
Enzyme 12 GenBank ID Protein Not Available
Enzyme 12 UniProtKB/Swiss-Prot ID A4D1D6 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name A4D1D6_HUMAN Link Image
Enzyme 12 PDB ID Not Available
Enzyme 12 Cellular Location Not Available
Enzyme 12 Gene Sequence Not Available
Enzyme 12 GenBank Gene ID CH236949 Link Image
Enzyme 12 GeneCard ID A4D1D6 Link Image
Enzyme 12 GenAtlas ID Not Available
Enzyme 12 HGNC ID Not Available
Enzyme 12 Chromosome Location Not Available
Enzyme 12 Locus Not Available
Enzyme 12 SNPs SNPJam Report Link Image
Enzyme 12 General References
  1. Scherer SW, Cheung J, MacDonald JR, Osborne LR, Nakabayashi K, Herbrick JA, Carson AR, Parker-Katiraee L, Skaug J, Khaja R, Zhang J, Hudek AK, Li M, Haddad M, Duggan GE, Fernandez BA, Kanematsu E, Gentles S, Christopoulos CC, Choufani S, Kwasnicka D, Zheng XH, Lai Z, Nusskern D, Zhang Q, Gu Z, Lu F, Zeesman S, Nowaczyk MJ, Teshima I, Chitayat D, Shuman C, Weksberg R, Zackai EH, Grebe TA, Cox SR, Kirkpatrick SJ, Rahman N, Friedman JM, Heng HH, Pelicci PG, Lo-Coco F, Belloni E, Shaffer LG, Pober B, Morton CC, Gusella JF, Bruns GA, Korf BR, Quade BJ, Ligon AH, Ferguson H, Higgins AW, Leach NT, Herrick SR, Lemyre E, Farra CG, Kim HG, Summers AM, Gripp KW, Roberts W, Szatmari P, Winsor EJ, Grzeschik KH, Teebi A, Minassian BA, Kere J, Armengol L, Pujana MA, Estivill X, Wilson MD, Koop BF, Tosi S, Moore GE, Boright AP, Zlotorynski E, Kerem B, Kroisel PM, Petek E, Oscier DG, Mould SJ, Dohner H, Dohner K, Rommens JM, Vincent JB, Venter JC, Li PW, Mural RJ, Adams MD, Tsui LC: Human chromosome 7: DNA sequence and biology. Science. 2003 May 2;300(5620):767-72. Epub 2003 Apr 10. [PubMed Link Image]
Enzyme 12 Metabolite References Not Available
Enzyme 13 [top]
Enzyme 13 ID 16472
Enzyme 13 Name cDNA, FLJ93082, Homo sapiens carnitine palmitoyltransferase II (CPT2), nuclear geneencoding mitochondrial protein, mRNA (Carnitine palmitoyltransferase II)
Enzyme 13 Synonyms Not Available
Enzyme 13 Gene Name CPT2
Enzyme 13 Protein Sequence >cDNA, FLJ93082, Homo sapiens carnitine palmitoyltransferase II (CPT2), nuclear geneencoding mitochondrial protein, mRNA (Carnitine palmitoyltransferase II) 
MVPRLLLRAWPRGPAVGPGAPSRPLSAGSGPGQYLQRSIVPTMHYQDSLPRLPIPKLEDT
IRRYLSAQKPLLNDGQFRKTEQFCKSFENGIGKELHEQLVALDKQNKHTSYISGPWFDMY
LSARDSVVLNFNPFMAFNPDPKSEYNDQLTRATNMTVSAIRFLKTLRAGLLEPEVFHLNP
AKSDTITFKRLIRFVPSSLSWYGAYLVNAYPLDMSQYFRLFNSTRLPKPSRDELFTDDKA
RHLLVLRKGNFYIFDVLDQDGNIVSPSEIQAHLKYILSDSSPAPEFPLAYLTSENRDIWA
ELRQKLMSSGNEESLRKVDSAVFCLCLDDFPIKDLVHLSHNMLHGDGTNRWFDKSFNLII
AKDGSTAVHFEHSWGDGVAVLRFFNEVFKDSTQTPAVTPQSQPATTDSTVTVQKLNFELT
DALKTGITAAKEKFDATMKTLTIDCVQFQRGGKEFLKKQKLSPDAVAQLAFQMAFLRQYG
QTVATYESCSTAAFKHGRTETIRPASVYTKRCSEAFVREPSRHSAGELQQMMVECSKYHG
QLTKEAAMGQGFDRHLFALRHLAAAKGIILPELYLDPAYGQINHNVLSTSTLSSPAVNLG
GFAPVVSDGFGVGYAVHDNWIGCNVSSYPGRNAREFLQCVEKALEDMFDALEGKSIKS
Enzyme 13 Number of Residues 658
Enzyme 13 Molecular Weight 73778
Enzyme 13 Theoretical pI 8.30
Enzyme 13 GO Classification
Function
  • acyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring groups other than amino-acyl groups
Process
—
Component
—
Enzyme 13 General Function Not Available
Enzyme 13 Specific Function Not Available
Enzyme 13 Pathways Not Available
Enzyme 13 Reactions Not Available
Enzyme 13 Pfam Domain Function
Enzyme 13 Signals
  • None
Enzyme 13 Transmembrane Regions
  • None
Enzyme 13 Essentiality Not Available
Enzyme 13 GenBank ID Protein Not Available
Enzyme 13 UniProtKB/Swiss-Prot ID B2R6S0 Link Image
Enzyme 13 UniProtKB/Swiss-Prot Entry Name B2R6S0_HUMAN Link Image
Enzyme 13 PDB ID Not Available
Enzyme 13 Cellular Location Not Available
Enzyme 13 Gene Sequence Not Available
Enzyme 13 GenBank Gene ID AK312687 Link Image
Enzyme 13 GeneCard ID B2R6S0 Link Image
Enzyme 13 GenAtlas ID Not Available
Enzyme 13 HGNC ID Not Available
Enzyme 13 Chromosome Location Not Available
Enzyme 13 Locus Not Available
Enzyme 13 SNPs SNPJam Report Link Image
Enzyme 13 General References Not Available
Enzyme 13 Metabolite References Not Available
Enzyme 14 [top]
Enzyme 14 ID 17028
Enzyme 14 Name Mitochondrial carnitine/acylcarnitine carrier protein CACL
Enzyme 14 Synonyms
  1. CACT-like
  2. Solute carrier family 25 member 29
Enzyme 14 Gene Name SLC25A29
Enzyme 14 Protein Sequence >Mitochondrial carnitine/acylcarnitine carrier protein CACL 
MALDFLAGCAGGVAGVLVGHPFDTVKVRLQVQSVEKPQYRGTLHCFKSIIKQESVLGLYK
GLGSPLMGLTFINALVFGVQGNTLRALGHDSPLNQFLAGAAAGAIQCVICCPMELAKTRL
QLQDAGPARTYKGSLDCLAQIYGHEGLRGVNRGMVSTLLRETPSFGVYFLTYDALTRALG
CEPGDRLLVPKLLLAGGTSGIVSWLSTYPVDVVKSRLQADGLRGAPRYRGILDCVHQSYR
AEGWRVFTRGLASTLLRAFPVNAATFATVTVVLTYARGEEAGPEGEAVPAAPAGPALAQP
SSL
Enzyme 14 Number of Residues 303
Enzyme 14 Molecular Weight 32063
Enzyme 14 Theoretical pI 8.89
Enzyme 14 GO Classification
Function
  • binding
  • transporter activity
Process
  • cellular physiological process
  • physiological process
  • transport
Component
  • cell
  • membrane
  • mitochondrial inner membrane
  • organelle inner membrane
  • organelle membrane
Enzyme 14 General Function Not Available
Enzyme 14 Specific Function Has palmitoylcarnitine transporting activity
Enzyme 14 Pathways Not Available
Enzyme 14 Reactions Not Available
Enzyme 14 Pfam Domain Function
Enzyme 14 Signals
  • None
Enzyme 14 Transmembrane Regions
  • 2-22 61-81 96-116 153-172 187-207 255-275
Enzyme 14 Essentiality Not Available
Enzyme 14 GenBank ID Protein Not Available
Enzyme 14 UniProtKB/Swiss-Prot ID Q8N8R3 Link Image
Enzyme 14 UniProtKB/Swiss-Prot Entry Name MCATL_HUMAN Link Image
Enzyme 14 PDB ID Not Available
Enzyme 14 Cellular Location Not Available
Enzyme 14 Gene Sequence Not Available
Enzyme 14 GenBank Gene ID BX247983 Link Image
Enzyme 14 GeneCard ID Q8N8R3 Link Image
Enzyme 14 GenAtlas ID SLC25A29 Link Image
Enzyme 14 HGNC ID HGNC:20116 Link Image
Enzyme 14 Chromosome Location 14
Enzyme 14 Locus 14q32.2
Enzyme 14 SNPs SNPJam Report Link Image
Enzyme 14 General References Not Available
Enzyme 14 Metabolite References Not Available