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Human Metabolome Database Version 2.5

 

Showing metabocard for L-Acetylcarnitine (HMDB00201)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-11-24 13:03:42
Accession Number HMDB00201
Secondary Accession Numbers HMDB00456; HMDB00515
Common Name L-Acetylcarnitine
Description An acetic acid ester of carnitine that facilitates movement of acetyl CoA into the matrices of mammalian mitochondria during the oxidation of fatty acids. In addition to his metabolic role, acetyl-L-carnitine (ALC) posses unique neuroprotective, neuromodulatory, and neurotrophic properties this may play an important role in counteracting various disease processes. (PubMed ID 15363640)
Synonyms
  1. (-)-Acetylcarnitine
  2. (R)-Acetylcarnitine
  3. ALCAR
  4. Acetyl-L-(-)-carnitine
  5. Acetyl-L-carnitine
  6. Acetylcarnitine
  7. L-Acetylcarnitine
  8. L-Carnitine acetyl ester
  9. L-O-Acetylcarnitine
  10. Levocarnitine acetyl
  11. Nicetile
  12. O-Acetyl-L-carnitine
  13. O-Acetylcarnitine
  14. (+-)-Acetylcarnitine
Chemical IUPAC Name (3S)-3-acetyloxy-4-trimethylammonio-butanoate
Chemical Formula C9H17NO4
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Amino acids and Amino Acid conjugates
Class
  • Quaternary Amines
Sub Class
  • Short chain acyl carnitines
Family
  • Mammalian Metabolite
Species
  • cation
  • anion
  • quaternary ammonium salt
  • carboxylic acid salt
  • carboxylic acid ester
Biofunction
  • Component of Alanine and aspartate metabolism
Application
—
Source
  • Endogenous
Average Molecular Weight 203.236
Monoisotopic Molecular Weight 203.115753
Isomeric SMILES CC(=O)OC(CC([O-])=O)C[N+](C)(C)C
Canonical SMILES CC(=O)OC(CC([O-])=O)C[N+](C)(C)C
KEGG Compound ID C02571 Link Image
BioCyc ID (-)o-acetylcarnitine Link Image
BiGG ID 1442845 Link Image
Wikipedia Link Acetyl-L-carnitine Link Image
NuGOwiki Link HMDB00201 Link Image
Metagene Link HMDB00201 Link Image
METLIN ID 5213 Link Image
PubChem Compound 18230 Link Image
PubChem Substance 11113462 Link Image
ChEBI ID Not Available
CAS Registry Number 3040-38-8
InChI Identifier InChI=1/C9H17NO4/c1-7(11)14-8(5-9(12)13)6-10(2,3)4/h8H,5-6H2,1-4H3
Synthesis Reference Gu, Heng-da; Shi, Shuang; Yang, Ying; Shi, Zhao-xin; Yu, Zhan-long. Synthesis of acetyl-L-carnitine by direct acylation method. Shenyang Huagong Xueyuan Xuebao (2006), 20(2), 154-155, 160.
Melting Point (Experimental) 145
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 0.355 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge 0
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -2.39 [Predicted by ALOGPS] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Experimental 13C NMR Spectrum Not Available
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
Show Experimental Conditions Link Image
High Energy
Download File
Show Experimental Conditions Link Image
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location
  • Cytoplasm
  • endoplasmic reticulum
  • mitochondria
  • peroxisome
Biofluid Location
  • Blood
  • Cerebrospinal Fluid
  • Urine
Tissue Location
Tissue References
Brain —
Muscle —
Nerve Cells —
Neuron —
Skeletal Muscle —
Spermatozoa —
Concentrations (Normal)
Biofluid Blood
Value 6.2 +/- 0.6 uM
Age Adult:>18 yrs old
Sex Male
Patient information Normal
Comments Not Available
References
  • Niu YJ, Jiang ZM, Shu H, Li CF, Liu W, Yao GX, Jiang J, Li JQ, Longo A: [Assay of carnitine in plasma and urine of healthy adults] Zhongguo Yi Xue Ke Xue Yuan Xue Bao. 2002 Apr;24(2):185-7. [PubMed Link Image]
Biofluid Blood
Value 5.7 +/- 0.7 uM
Age Adult:>18 yrs old
Sex Female
Patient information Normal
Comments Not Available
References
  • Niu YJ, Jiang ZM, Shu H, Li CF, Liu W, Yao GX, Jiang J, Li JQ, Longo A: [Assay of carnitine in plasma and urine of healthy adults] Zhongguo Yi Xue Ke Xue Yuan Xue Bao. 2002 Apr;24(2):185-7. [PubMed Link Image]
Biofluid Blood
Value 4.90 (2.48-8.62) uM
Age Children:1-13 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Costa CG, Struys EA, Bootsma A, ten Brink HJ, Dorland L, Tavares de Almeida I, Duran M, Jakobs C: Quantitative analysis of plasma acylcarnitines using gas chromatography chemical ionization mass fragmentography. J Lipid Res. 1997 Jan;38(1):173-82. [PubMed Link Image]
Biofluid CSF
Value 0.322 +/- 0.148 uM
Age Adult:>18 yrs old
Sex N/A
Patient information Normal
Comments Not Available
References
Biofluid Urine
Value 1.928 +/- 0.2829 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Female
Patient information Normal
Comments Not Available
References
  • Niu YJ, Jiang ZM, Shu H, Li CF, Liu W, Yao GX, Jiang J, Li JQ, Longo A: [Assay of carnitine in plasma and urine of healthy adults] Zhongguo Yi Xue Ke Xue Yuan Xue Bao. 2002 Apr;24(2):185-7. [PubMed Link Image]
Concentrations (Abnormal)
Biofluid Blood
Value 0.316 (0.091-0.760) uM
Age Adult:>18 yrs old
Sex Both
Condition Very Long Chain Acyl-CoA Dehydrogenase Deficiency
Comments Not Available
References
  • Costa CG, Struys EA, Bootsma A, ten Brink HJ, Dorland L, Tavares de Almeida I, Duran M, Jakobs C: Quantitative analysis of plasma acylcarnitines using gas chromatography chemical ionization mass fragmentography. J Lipid Res. 1997 Jan;38(1):173-82. [PubMed Link Image]
Associated Disorders
Condition References
Very Long Chain Acyl-CoA Dehydrogenase Deficiency
  • Costa CG, Struys EA, Bootsma A, ten Brink HJ, Dorland L, Tavares de Almeida I, Duran M, Jakobs C: Quantitative analysis of plasma acylcarnitines using gas chromatography chemical ionization mass fragmentography. J Lipid Res. 1997 Jan;38(1):173-82. [PubMed Link Image]
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Beta Oxidation of Very Long Chain Fatty Acids SMP00052 Link Image map01040 Link Image
Oxidation of Branched Chain Fatty Acids SMP00030 Link Image
General References
  1. Sakuma T: Alteration of urinary carnitine profile induced by benzoate administration. Arch Dis Child. 1991 Jul;66(7):873-5. [PubMed Link Image]
  2. Grizard G, Lombard-Vignon N, Boucher D: Changes in carnitine and acetylcarnitine in human semen during cryopreservation. Hum Reprod. 1992 Oct;7(9):1245-8. [PubMed Link Image]
  3. Kamimori H, Hamashima Y, Konishi M: Determination of carnitine and saturated-acyl group carnitines in human urine by high-performance liquid chromatography with fluorescence detection. Anal Biochem. 1994 May 1;218(2):417-24. [PubMed Link Image]
  4. Cooper MB, Forte CA, Jones DA: Citrate interference with the determination of acetylcarnitine: a method for its elimination. Clin Chim Acta. 1986 Sep 30;159(3):291-9. [PubMed Link Image]
  5. Spagnoli A, Lucca U, Menasce G, Bandera L, Cizza G, Forloni G, Tettamanti M, Frattura L, Tiraboschi P, Comelli M, et al.: Long-term acetyl-L-carnitine treatment in Alzheimer's disease. Neurology. 1991 Nov;41(11):1726-32. [PubMed Link Image]
  6. Brooks DE: Carnitine, acetylcarnitine and the activity of carnitine acyltransferases in seminal plasma and spermatozoa of men, rams and rats. J Reprod Fertil. 1979 Jul;56(2):667-73. [PubMed Link Image]
  7. Inoue F, Terada N, Nakajima H, Okochi M, Kodo N, Kizaki Z, Kinugasa A, Sawada T: Effect of sports activity on carnitine metabolism. Measurement of free carnitine, gamma-butyrobetaine and acylcarnitines by tandem mass spectrometry. J Chromatogr B Biomed Sci Appl. 1999 Aug 6;731(1):83-8. [PubMed Link Image]
  8. Niu YJ, Jiang ZM, Shu H, Li CF, Liu W, Yao GX, Jiang J, Li JQ, Longo A: [Assay of carnitine in plasma and urine of healthy adults] Zhongguo Yi Xue Ke Xue Yuan Xue Bao. 2002 Apr;24(2):185-7. [PubMed Link Image]
  9. Siliprandi N, Di Lisa F, Pieralisi G, Ripari P, Maccari F, Menabo R, Giamberardino MA, Vecchiet L: Metabolic changes induced by maximal exercise in human subjects following L-carnitine administration. Biochim Biophys Acta. 1990 Apr 23;1034(1):17-21. [PubMed Link Image]
  10. Marzo A, Cardace G, Corbelleta C, Bassani E, Morabito E, Arrigoni Martelli E: Homeostatic equilibrium of L-carnitine family before and after i.v. administration of propionyl-L-carnitine in humans, dogs and rats. Eur J Drug Metab Pharmacokinet. 1991;Spec No 3:357-63. [PubMed Link Image]
  11. Novak M, Wieser PB, Buch M, Hahn P: Acetylcarnitine and free carnitine in body fluids before and after birth. Pediatr Res. 1979 Jan;13(1):10-5. [PubMed Link Image]
  12. Battistin L, Pizzolato G, Dam M, Da Col C, Perlotto N, Saitta B, Borsato N, Calvani M, Ferlin G: Single-photon emission computed tomography studies with 99mTc-hexamethylpropyleneamine oxime in dementia: effects of acute administration of L-acetylcarnitine. Eur Neurol. 1989;29(5):261-5. [PubMed Link Image]
  13. Deufel T: Determination of L-carnitine in biological fluids and tissues. J Clin Chem Clin Biochem. 1990 May;28(5):307-11. [PubMed Link Image]
  14. Minkler PE, Hoppel CL: Quantification of free carnitine, individual short- and medium-chain acylcarnitines, and total carnitine in plasma by high-performance liquid chromatography. Anal Biochem. 1993 Aug 1;212(2):510-8. [PubMed Link Image]
  15. Bruno G, Scaccianoce S, Bonamini M, Patacchioli FR, Cesarino F, Grassini P, Sorrentino E, Angelucci L, Lenzi GL: Acetyl-L-carnitine in Alzheimer disease: a short-term study on CSF neurotransmitters and neuropeptides. Alzheimer Dis Assoc Disord. 1995 Fall;9(3):128-31. [PubMed Link Image]
  16. Pace S, Longo A, Toon S, Rolan P, Evans AM: Pharmacokinetics of propionyl-L-carnitine in humans: evidence for saturable tubular reabsorption. Br J Clin Pharmacol. 2000 Nov;50(5):441-8. [PubMed Link Image]
  17. De Rosa M, Boggia B, Amalfi B, Zarrilli S, Vita A, Colao A, Lombardi G: Correlation between seminal carnitine and functional spermatozoal characteristics in men with semen dysfunction of various origins. Drugs R D. 2005;6(1):1-9. [PubMed Link Image]
  18. Zanelli SA, Solenski NJ, Rosenthal RE, Fiskum G: Mechanisms of ischemic neuroprotection by acetyl-L-carnitine. Ann N Y Acad Sci. 2005 Aug;1053:153-61. [PubMed Link Image]
  19. Kuratsune H, Yamaguti K, Lindh G, Evengard B, Hagberg G, Matsumura K, Iwase M, Onoe H, Takahashi M, Machii T, Kanakura Y, Kitani T, Langstrom B, Watanabe Y: Brain regions involved in fatigue sensation: reduced acetylcarnitine uptake into the brain. Neuroimage. 2002 Nov;17(3):1256-65. [PubMed Link Image]
  20. Gray SC, Devito G, Nimmo MA: Effect of active warm-up on metabolism prior to and during intense dynamic exercise. Med Sci Sports Exerc. 2002 Dec;34(12):2091-6. [PubMed Link Image]
  21. Wikipedia Link Image
Metabolic Enzymes
  1. Carnitine O-acetyltransferase
  2. Mitochondrial carnitine/acylcarnitine carrier protein
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 8300
Enzyme 2 Name Mitochondrial carnitine/acylcarnitine carrier protein
Enzyme 2 Synonyms
  1. Carnitine/acylcarnitine translocase
  2. CAC
  3. Solute carrier family 25 member 20
Enzyme 2 Gene Name SLC25A20
Enzyme 2 Protein Sequence >Mitochondrial carnitine/acylcarnitine carrier protein 
MADQPKPISPLKNLLAGGFGGVCLVFVGHPLDTVKVRLQTQPPSLPGQPPMYSGTFDCFR
KTLFREGITGLYRGMAAPIIGVTPMFAVCFFGFGLGKKLQQKHPEDVLSYPQLFAAGMLS
GVFTTGIMTPGERIKCLLQIQASSGESKYTGTLDCAKKLYQEFGIRGIYKGTVLTLMRDV
PASGMYFMTYEWLKNIFTPEGKRVSELSAPRILVAGGIAGIFNWAVAIPPDVLKSRFQTA
PPGKYPNGFRDVLRELIRDEGVTSLYKGFNAVMIRAFPANAACFLGFEVAMKFLNWATPN
L
Enzyme 2 Number of Residues 301
Enzyme 2 Molecular Weight 32944
Enzyme 2 Theoretical pI 9.84
Enzyme 2 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 2 General Function Not Available
Enzyme 2 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 2 Pathways Not Available
Enzyme 2 Reactions Not Available
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • 13-31 74-93 113-131 171-190 212-230 268-287
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 2765075 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID O43772 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name MCAT_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >906 bp 
ATGGCCGACCAGCCAAAACCCATCAGCCCGCTCAAGAACCTGCTGGCCGGCGGCTTTGGC
GGCGTGTGCCTGGTGTTCGTCGGTCACCCTCTGGACACGGTCAAGGTCCGACTGCAGACA
CAGCCACCGAGTTTGCCTGGACAACCTCCCATGTACTCTGGGACCTTTGACTGTTTCCGG
AAGACTCTTTTTAGAGAGGGCATCACGGGGCTATATCGGGGAATGGCTGCCCCTATCATC
GGGGTCACTCCCATGTTTGCCGTGTGCTTCTTTGGGTTTGGTTTGGGGAAGAAACTACAA
CAGAAACACCCAGAAGATGTGCTCAGCTATCCCCAGCTTTTTGCAGCTGGGATGTTATCT
GGCGTATTCACCACAGGAATCATGACTCCTGGAGAACGGATCAAGTGCTTATTACAGATT
CAGGCTTCTTCAGGAGAAAGCAAGTACACTGGTACCTTGGACTGTGCAAAGAAGCTGTAC
CAGGAGTTTGGGATCCGAGGCATCTACAAAGGGACTGTGCTTACCCTTATGCGAGATGTC
CCAGCTAGTGGAATGTATTTCATGACATATGAATGGCTGAAAAATATCTTCACTCCGGAG
GGAAAGAGGGTCAGTGAGCTCAGTGCCCCTCGGATCTTGGTGGCTGGGGGCATTGCAGGG
ATCTTCAACTGGGCTGTGGCAATCCCCCCAGATGTGCTCAAGTCTCGATTCCAGACTGCA
CCTCCTGGGAAATATCCTAATGGTTTCAGAGATGTGCTGAGGGAGCTGATCCGGGATGAA
GGAGTCACATCCTTGTACAAAGGGTTCAATGCAGTGATGATCCGAGCCTTCCCAGCCAAT
GCGGCCTGTTTCCTTGGCTTTGAAGTTGCCATGAAGTTCCTTAATTGGGCCACCCCCAAC
TTGTGA
Enzyme 2 GenBank Gene ID Y10319 Link Image
Enzyme 2 GeneCard ID SLC25A20 Link Image
Enzyme 2 GenAtlas ID SLC25A20 Link Image
Enzyme 2 HGNC ID HGNC:1421 Link Image
Enzyme 2 Chromosome Location 3
Enzyme 2 Locus 3p21.31
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 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 2 Metabolite References Not Available