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Human Metabolome Database Version 2.5

 

Showing metabocard for L-Palmitoylcarnitine (HMDB00222)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-05-05 20:57:46
Accession Number HMDB00222
Secondary Accession Numbers HMDB00846
Common Name L-Palmitoylcarnitine
Description L-Palmitoylcarnitine is a long-chain acyl fatty acid derivative ester of carnitine which facilitates the transfer of long-chain fatty acids from cytoplasm into mitochondria during the oxidation of fatty acids. L-palmitoylcarnitine, due to its amphipatic character is, like detergents, a surface-active molecule and by changing the membrane fluidity and surface charge can change activity of several enzymes and transporters localized in the membrane. L-palmitoylcarnitine has been also reported to change the activity of certain proteins. On the contrary to carnitine, palmitoylcarnitine was shown to stimulate the activity of caspases 3, 7 and 8 and the level of this long-chain acylcarnitine increased during apoptosis. Palmitoylcarnitine was also reported to diminish completely binding of phorbol esters, the protein kinase C activators and to decrease the autophosphorylation of the enzyme. Apart from these isoform nonspecific phenomena, palmitoylcarnitine was also shown to be responsible for retardation in cytoplasm of protein kinase C isoforms β and δ and, in the case of the latter one, to decrease its interaction with GAP-43. Some of the physico-chemical properties of palmitoylcarnitine may help to explain the need for coenzyme A-carnitine-coenzyme A acyl exchange during mitochondrial fatty acid import. The amphiphilic character of palmitoylcarnitine may also explain its proposed involvement in the pathogenesis of myocardial ischemia. L-Palmitoylcarnitine accumulates in ischemic myocardium and potentially contribute to myocardial damage through alterations in membrane molecular dynamics , one mechanism through which could play an important role in ischemic injury. Palmitoylcarnitine is characteristically elevated in carnitine palmitoyltransferase II deficiency, late-onset (OMIM 255110). (PMID 2540838, 15363641, 8706815)
Synonyms
  1. Palmitoyl d-carnitine
  2. (3S)-3-hexadecanoyloxy-4-(trimethylammonio)butanoate
  3. (3S)-3-hexadecanoyloxy-4-(trimethylammonio)butanoic acid
  4. L-carnitine palmitoyl ester
  5. (+)-palmitoylcarnitine
  6. Hexadecanoyl-L-carnitine
  7. (3S)-3-palmitoyloxy-4-(trimethylammonio)butanoate
  8. (3S)-3-palmitoyloxy-4-(trimethylammonio)butanoic acid
  9. Palmityl-L-carnitine
  10. D-palmitylcarnitine
  11. L-palmitoyl-L-carnitine
  12. Hexadecenoyl carnitine
  13. L(-)-Palmitylcarnitine
  14. Palmitoyl-(-)-carnitine
  15. Palmitoyl-L-carnitine
  16. 3-carboxy-N,N,N-trimethyl-2-[(1-oxohexadecyl)oxy]-1-Propanaminium
Chemical IUPAC Name (3R)-3-hexadecanoyloxy-4-trimethylazaniumylbutanoate
Chemical Formula C23H45NO4
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Amino acids and Amino Acid conjugates
Class
  • Quaternary Amines
Sub Class
  • Long chain acyl carnitines
Family
  • Mammalian Metabolite
Species
  • cation
  • anion
  • quaternary ammonium salt
  • carboxylic acid salt
  • carboxylic acid ester
Biofunction
  • Component of Fatty acid metabolism
Application
—
Source
  • Endogenous
Average Molecular Weight 399.608
Monoisotopic Molecular Weight 399.334869
Isomeric SMILES CCCCCCCCCCCCCCCC(=O)O[C@H](CC([O-])=O)C[N+](C)(C)C
Canonical SMILES CCCCCCCCCCCCCCCC(=O)OC(CC([O-])=O)C[N+](C)(C)C
KEGG Compound ID C02990 Link Image
BioCyc ID CPD-419 Link Image
BiGG ID 40966 Link Image
Wikipedia Link Not Available
NuGOwiki Link HMDB00222 Link Image
Metagene Link HMDB00222 Link Image
METLIN ID 5231 Link Image
PubChem Compound 11953816 Link Image
PubChem Substance 24701436 Link Image
ChEBI ID 17490 Link Image
CAS Registry Number 2364-67-2
InChI Identifier InChI=1/C23H45NO4/c1-5-6-7-8-9-10-11-12-13-14-15-16-17-18-23(27)28-21(19-22(25)26)20-24(2,3)4/h21H,5-20H2,1-4H3/t21-/m1/s1
Synthesis Reference Norum, Kaare R. Palmityl coenzyme A-carnitine palmityltransferase. Purification from calf-liver mitochondria and some properties of the enzyme. Biochimica et Biophysica Acta, Specialized Section on Enzymological Subjects (1964), 89(1), 95-108.
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 1.20e-05 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge 0
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity 1.77 [Predicted by ALOGPS] Calculated using ALOGPS
Material Safety Data Sheet (MSDS) Not Available
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 (Varian)
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
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High Energy
Download File
Show Experimental Conditions Link Image
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location
  • Cytoplasm
  • mitochondria
Biofluid Location
  • Blood
  • Urine
Tissue Location Not Available
Concentrations (Normal)
Biofluid Blood
Value 0.113 +/- 0.006 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Bene J, Komlosi K, Gasztonyi B, Juhasz M, Tulassay Z, Melegh B: Plasma carnitine ester profile in adult celiac disease patients maintained on long-term gluten free diet. World J Gastroenterol. 2005 Nov 14;11(42):6671-5. [PubMed Link Image]
Biofluid Blood
Value 0.153 (0.073-0.227) 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 Urine
Value 0.5 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Mueller P, Schulze A, Schindler I, Ethofer T, Buehrdel P, Ceglarek U: Validation of an ESI-MS/MS screening method for acylcarnitine profiling in urine specimens of neonates, children, adolescents and adults. Clin Chim Acta. 2003 Jan;327(1-2):47-57. [PubMed Link Image]
Concentrations (Abnormal)
Biofluid Blood
Value 0.097 +/- 0.006 uM
Age Adult:>18 yrs old
Sex Both
Condition Celiac disease
Comments Not Available
References
  • Bene J, Komlosi K, Gasztonyi B, Juhasz M, Tulassay Z, Melegh B: Plasma carnitine ester profile in adult celiac disease patients maintained on long-term gluten free diet. World J Gastroenterol. 2005 Nov 14;11(42):6671-5. [PubMed Link Image]
Biofluid Blood
Value 1.909 (1.012-2.233) 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
Celiac disease
  • Bene J, Komlosi K, Gasztonyi B, Juhasz M, Tulassay Z, Melegh B: Plasma carnitine ester profile in adult celiac disease patients maintained on long-term gluten free diet. World J Gastroenterol. 2005 Nov 14;11(42):6671-5. [PubMed Link Image]
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
Pathways
Name SMPDB Link KEGG Link
Fatty acid Metabolism SMP00051 Link Image map00071 Link Image
General References
  1. Mueller P, Schulze A, Schindler I, Ethofer T, Buehrdel P, Ceglarek U: Validation of an ESI-MS/MS screening method for acylcarnitine profiling in urine specimens of neonates, children, adolescents and adults. Clin Chim Acta. 2003 Jan;327(1-2):47-57. [PubMed Link Image]
  2. 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]
  3. Moder M, Kiessling A, Loster H, Bruggemann L: The pattern of urinary acylcarnitines determined by electrospray mass spectrometry: a new tool in the diagnosis of diabetes mellitus. Anal Bioanal Chem. 2003 Jan;375(2):200-10. Epub 2003 Jan 4. [PubMed Link Image]
  4. Wasant P, Matsumoto I, Naylor E, Liammongkolkul S: Mitochondrial fatty acid oxidation disorders in Thai infants: a report of 3 cases. J Med Assoc Thai. 2002 Aug;85 Suppl 2:S710-9. [PubMed Link Image]
  5. Young SP, Matern D, Gregersen N, Stevens RD, Bali D, Liu HM, Koeberl DD, Millington DS: A comparison of in vitro acylcarnitine profiling methods for the diagnosis of classical and variant short chain acyl-CoA dehydrogenase deficiency. Clin Chim Acta. 2003 Nov;337(1-2):103-13. [PubMed Link Image]
  6. Poorthuis BJ, Jille-Vlckova T, Onkenhout W: Determination of acylcarnitines in urine of patients with inborn errors of metabolism using high-performance liquid chromatography after derivatization with 4'-bromophenacylbromide. Clin Chim Acta. 1993 Jul 16;216(1-2):53-61. [PubMed Link Image]
  7. Bhuiyan AK, Jackson S, Turnbull DM, Aynsley-Green A, Leonard JV, Bartlett K: The measurement of carnitine and acyl-carnitines: application to the investigation of patients with suspected inherited disorders of mitochondrial fatty acid oxidation. Clin Chim Acta. 1992 May 15;207(3):185-204. [PubMed Link Image]
Metabolic Enzymes
  1. Carnitine O-palmitoyltransferase I, muscle isoform
  2. Carnitine O-palmitoyltransferase I, liver isoform
  3. Long-chain-fatty-acid--CoA ligase 1
  4. Carnitine acyltransferase-like protein 1
  5. cDNA, FLJ93082, Homo sapiens carnitine palmitoyltransferase II (CPT2), nuclear geneencoding mitochondrial protein, mRNA (Carnitine palmitoyltransferase II)
Enzyme 1 [top]
Enzyme 1 ID 5543
Enzyme 1 Name Carnitine O-palmitoyltransferase I, muscle isoform
Enzyme 1 Synonyms
  1. CPT I
  2. CPTI-M
  3. Carnitine palmitoyltransferase 1B
  4. Carnitine palmitoyltransferase I-like protein
Enzyme 1 Gene Name CPT1B
Enzyme 1 Protein Sequence >Carnitine O-palmitoyltransferase I, muscle isoform 
MAEAHQAVAFQFTVTPDGVDFRLSREALKHVYLSGINSWKKRLIRIKNGILRGVYPGSPT
SWLVVIMATVGSSFCNVDISLGLVSCIQRCLPQGCGPYQTPQTRALLSMAIFSTGVWVTG
IFFFRQTLKLLLCYHGWMFEMHGKTSNLTRIWAMCIRLLSSRHPMLYSFQTSLPKLPVPR
VSATIQRYLESVRPLLDDEEYYRMELLAKEFQDKTAPRLQKYLVLKSWWASNYVSDWWEE
YIYLRGRSPLMVNSNYYVMDLVLIKNTDVQAARLGNIIHAMIMYRRKLDREEIKPVMALG
IVPMCSYQMERMFNTTRIPGKDTDVLQHLSDSRHVAVYHKGRFFKLWLYEGARLLKPQDL
EMQFQRILDDPSPPQPGEEKLAALTAGGRVEWAQARQAFFSSGKNKAALEAIERAAFFVA
LDEESYSYDPEDEASLSLYGKALLHGNCYNRWFDKSFTLISFKNGQLGLNAEHAWADAPI
IGHLWEFVLGTDSFHLGYTETGHCLGKPNPALAPPTRLQWDIPKQCQAVIESSYQVAKAL
ADDVELYCFQFLPFGKGLIKKCRTSPDAFVQIALQLAHFRDRGKFCLTYEASMTRMFREG
RTETVRSCTSESTAFVQAMMEGSHTKADLRDLFQKAAKKHQNMYRLAMTGAGIDRHLFCL
YLVSKYLGVSSPFLAEVLSEPWRLSTSQIPQSQIRMFDPEQHPNHLGAGGGFGPVADDGY
GVSYMIAGENTIFFHISSKFSSSETNAQRFGNHIRKALLDIADLFQVPKAYS
Enzyme 1 Number of Residues 772
Enzyme 1 Molecular Weight 87802
Enzyme 1 Theoretical pI 8.77
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 Palmitoyl-CoA + L-carnitine = CoA + L- palmitoylcarnitine
Enzyme 1 Pathways
Enzyme 1 Reactions
  • palmitoyl-CoA + L-carnitine = CoA + L-palmitoylcarnitine
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • 48-73 103-122
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 1621202 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID Q92523 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name CPT1B_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 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 1 GenBank Gene ID D87812 Link Image
Enzyme 1 GeneCard ID CPT1B Link Image
Enzyme 1 GenAtlas ID CPT1B Link Image
Enzyme 1 HGNC ID HGNC:2329 Link Image
Enzyme 1 Chromosome Location 22
Enzyme 1 Locus 22q13.33
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 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 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5544
Enzyme 2 Name Carnitine O-palmitoyltransferase I, liver isoform
Enzyme 2 Synonyms
  1. CPT I
  2. CPTI-L
  3. Carnitine palmitoyltransferase 1A
Enzyme 2 Gene Name CPT1A
Enzyme 2 Protein Sequence >Carnitine O-palmitoyltransferase I, liver isoform 
MAEAHQAVAFQFTVTPDGIDLRLSHEALRQIYLSGLHSWKKKFIRFKNGIITGVYPASPS
SWLIVVVGVMTTMYAKIDPSLGIIAKINRTLETANCMSSQTKNVVSGVLFGTGLWVALIV
TMRYSLKVLLSYHGWMFTEHGKMSRATKIWMGMVKIFSGRKPMLYSFQTSLPRLPVPAVK
DTVNRYLQSVRPLMKEEDFKRMTALAQDFAVGLGPRLQWYLKLKSWWATNYVSDWWEEYI
YLRGRGPLMVNSNYYAMDLLYILPTHIQAARAGNAIHAILLYRRKLDREEIKPIRLLGST
IPLCSAQWERMFNTSRIPGEETDTIQHMRDSKHIVVYHRGRYFKVWLYHDGRLLKPREME
QQMQRILDNTSEPQPGEARLAALTAGDRVPWARCRQAYFGRGKNKQSLDAVEKAAFFVTL
DETEEGYRSEDPDTSMDSYAKSLLHGRCYDRWFDKSFTFVVFKNGKMGLNAEHSWADAPI
VAHLWEYVMSIDSLQLGYAEDGHCKGDINPNIPYPTRLQWDIPGECQEVIETSLNTANLL
ANDVDFHSFPFVAFGKGIIKKCRTSPDAFVQLALQLAHYKDMGKFCLTYEASMTRLFREG
RTETVRSCTTESCDFVRAMVDPAQTVEQRLKLFKLASEKHQHMYRLAMTGSGIDRHLFCL
YVVSKYLAVESPFLKEVLSEPWRLSTSQTPQQQVELFDLENNPEYVSSGGGFGPVADDGY
GVSYILVGENLINFHISSKFSCPETDSHRFGRHLKEAMTDIITLFGLSSNSKK
Enzyme 2 Number of Residues 773
Enzyme 2 Molecular Weight 88369
Enzyme 2 Theoretical pI 8.84
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 Palmitoyl-CoA + L-carnitine = CoA + L- palmitoylcarnitine
Enzyme 2 Pathways
Enzyme 2 Reactions
  • palmitoyl-CoA + L-carnitine = CoA + L-palmitoylcarnitine
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • 48-73 103-122
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 755646 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P50416 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name CPT1A_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 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 2 GenBank Gene ID L39211 Link Image
Enzyme 2 GeneCard ID CPT1A Link Image
Enzyme 2 GenAtlas ID CPT1A Link Image
Enzyme 2 HGNC ID HGNC:2328 Link Image
Enzyme 2 Chromosome Location 11
Enzyme 2 Locus 11q13.1-q13.2
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 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 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5849
Enzyme 3 Name Long-chain-fatty-acid--CoA ligase 1
Enzyme 3 Synonyms
  1. Long-chain acyl-CoA synthetase 1
  2. LACS 1
  3. Palmitoyl-CoA ligase 1
  4. Long-chain fatty acid CoA ligase 2
  5. Long-chain acyl-CoA synthetase 2
  6. LACS 2
  7. Acyl-CoA synthetase 1
  8. ACS1
  9. Palmitoyl-CoA ligase 2
Enzyme 3 Gene Name ACSL1
Enzyme 3 Protein Sequence >Long-chain-fatty-acid--CoA ligase 1 
MQAHELFRYFRMPELVDFRQYVRTLPTNTLMGFGAFAALTTFWYATRPKPLKPPCDLSMQ
SVEVAGSGGARRSALLDSDEPLVYFYDDVTTLYEGFQRGIQVSNNGPCLGSRKPDQPYEW
LSYKQVAELSECIGSALIQKGFKTAPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDT
LGNEAITYIVNKAELSLVFVDKPEKAKLLLEGVENKLIPGLKIIVVMDAYGSELVERGQR
CGVEVTSMKAMEDLGRANRRKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAF
VKATENTVNPCPDDTLISFLPLAHMFERVVECVMLCHGAKIGFFQGDIRLLMDDLKVLQP
TVFPVVPRLLNRMFDRIFGQANTTLKRWLLDFASKRKEAELRSGIIRNNSLWDRLIFHKV
QSSLGGRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWTAGHV
GAPMPCNLIKLVDVEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGD
IGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYMRSEPVAQVFVHGESLQAFLIAI
VVPDVETLCSWAQKRGFEGSFEELCRNKDVKKAILEDMVRLGKDSGLKPFEQVKGITLHP
ELFSIDNGLLTPTMKAKRPELRNYFRSQIDDLYSTIKV
Enzyme 3 Number of Residues 698
Enzyme 3 Molecular Weight 77944
Enzyme 3 Theoretical pI 7.16
Enzyme 3 GO Classification
Function
  • catalytic activity
Process
  • metabolism
  • physiological process
Component
—
Enzyme 3 General Function Lipid transport and metabolism
Enzyme 3 Specific Function Activation of long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. Preferentially uses palmitoleate, oleate and linoleate
Enzyme 3 Pathways
Enzyme 3 Reactions
  • ATP + a long-chain carboxylic acid + CoA = AMP + diphosphate + an acyl-CoA
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • 25-45
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 219900 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID P33121 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name ACSL1_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >2097 bp 
ATGCAAGCCCATGAGCTGTTCCGGTATTTTCGAATGCCAGAGCTGGTTGACTTCCGACAG
TACGTGCGTACTCTTCCGACCAACACGCTTATGGGCTTCGGAGCTTTTGCAGCACTCACC
ACCTTCTGGTACGCCACGAGACCCAAACCCCTGAAGCCGCCATGCGACCTCTCCATGCAG
TCAGTGGAAGTGGCGGGTAGTGGTGGTGCACGAAGATCCGCACTACTTGACAGCGACGAG
CCCTTGGTGTATTTCTATGATGATGTCACAACATTATACGAAGGTTTCCAGAGGGGAATA
CAGGTGTCAAATAATGGCCCTTGTTTAGGCTCTCGGAAACCAGACCAACCCTATGAATGG
CTTTCATATAAACAGGTTGCAGAATTGTCGGAGTGCATAGGCTCAGCACTGATCCAGAAG
GGCTTCAAGACTGCCCCAGATCAGTTCATTGGCATCTTTGCTCAAAATAGACCTGAGTGG
GTGATTATTGAACAAGGATGCTTTGCTTATTCGATGGTGATCGTTCCACTTTATGATACC
CTTGGAAATGAAGCCATCACGTACATAGTCAACAAAGCTGAACTCTCTCTGGTTTTTGTT
GACAAGCCAGAGAAGGCCAAACTCTTATTAGAGGGTGTAGAAAATAAGTTAATACCAGGC
CTTAAAATCATAGTTGTCATGGATGCCTACGGCAGTGAACTGGTGGAACGAGGCCAGAGG
TGTGGGGTGGAAGTCACCAGCATGAAGGCGATGGAGGACCTGGGAAGAGCCAACAGACGG
AAGCCCAAGCCTCCAGCACCTGAAGATCTTGCAGTAATTTGTTTCACAAGTGGAACTACA
GGCAACCCCAAAGGAGCAATGGTCACTCACCGAAACATAGTGAGCGATTGTTCAGCTTTT
GTGAAAGCAACAGAGAATACAGTCAATCCTTGCCCAGATGATACTTTGATATCTTTCTTG
CCTCTCGCCCATATGTTTGAGAGAGTTGTAGAGTGTGTAATGCTGTGTCATGGAGCTAAA
ATCGGATTTTTCCAAGGAGATATCAGGCTGCTCATGGATGACCTCAAGGTGCTTCAACCC
ACTGTCTTCCCCGTGGTTCCAAGACTGCTGAACCGGATGTTTGACCGAATTTTCGGACAA
GCAAACACCACGCTGAAGCGATGGCTCTTGGACTTTGCCTCCAAGAGGAAAGAAGCAGAG
CTTCGCAGCGGCATCATCAGAAACAACAGCCTGTGGGACCGGCTGATCTTCCACAAAGTA
CAGTCGAGCCTGGGCGGAAGAGTCCGGCTGATGGTGACAGGAGCCGCCCCGGTGTCTGCC
ACTGTGCTGACGTTCCTCAGAGCAGCCCTGGGCTGTCAGTTTTATGAAGGATACGGACAG
ACAGAGTGCACTGCCGGGTGCTGCCTAACCATGCCTGGAGACTGGACCGCAGGCCATGTT
GGGGCCCCGATGCCGTGCAATTTGATAAAACTTGTTGATGTGGAAGAAATGAATTACATG
GCTGCCGAGGGCGAGGGCGAGGTGTGTGTGAAAGGGCCAAATGTATTTCAGGGCTACTTG
AAGGACCCAGCGAAAACAGCAGAAGCTTTGGACAAAGACGGCTGGTTACACACAGGGGAC
ATTGGAAAATGGTTACCAAATGGCACCTTGAAAATTATCGACCGGAAAAAGCACATATTT
AAGCTGGCACAAGGAGAATACATAGCCCCTGAAAAGATTGAAAATATCTACATGCGAAGT
GAGCCTGTTGCTCAGGTGTTTGTCCACGGAGAAAGCCTGCAGGCATTTCTCATTGCAATT
GTGGTACCAGATGTTGAGACATTATGTTCCTGGGCCCAAAAGAGAGGATTTGAAGGGTCG
TTTGAGGAACTGTGCAGAAATAAGGATGTCAAAAAAGCTATCCTCGAAGATATGGTGAGA
CTTGGGAAGGATTCTGGTCTGAAACCATTTGAACAGGTCAAAGGCATCACATTGCACCCT
GAATTATTTTCTATCGACAATGGCCTTCTGACTCCAACAATGAAGGCGAAAAGGCCAGAG
CTGCGGAACTATTTCAGGTCGCAGATAGATGACCTCTATTCCACTATCAAGGTTTAG
Enzyme 3 GenBank Gene ID D10040 Link Image
Enzyme 3 GeneCard ID ACSL1 Link Image
Enzyme 3 GenAtlas ID ACSL1 Link Image
Enzyme 3 HGNC ID HGNC:3569 Link Image
Enzyme 3 Chromosome Location 4
Enzyme 3 Locus 4q34-q35
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Abe T, Fujino T, Fukuyama R, Minoshima S, Shimizu N, Toh H, Suzuki H, Yamamoto T: Human long-chain acyl-CoA synthetase: structure and chromosomal location. J Biochem (Tokyo). 1992 Jan;111(1):123-8. [PubMed Link Image]
  2. Ghosh B, Barbosa E, Singh I: Molecular cloning and sequencing of human palmitoyl-CoA ligase and its tissue specific expression. Mol Cell Biochem. 1995 Oct 4;151(1):77-81. [PubMed Link Image]
  3. Malhotra KT, Malhotra K, Lubin BH, Kuypers FA: Identification and molecular characterization of acyl-CoA synthetase in human erythrocytes and erythroid precursors. Biochem J. 1999 Nov 15;344 Pt 1:135-43. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 8763
Enzyme 4 Name Carnitine acyltransferase-like protein 1
Enzyme 4 Synonyms Not Available
Enzyme 4 Gene Name CATL1
Enzyme 4 Protein Sequence >Carnitine acyltransferase-like protein 1 
MAEAHQAVGFRPSLTSDGAEVELSAPVLQEIYLSGLRSWKRHLSRFWNDFLTGVFPASPL
SWLFLFSAIQLAWFLQLDPSLGLMEKIKELLPDWGGQHHGLRGVLAAALFASCLWGALIF
TLHVALRLLLSYHGWLLEPHGAMSSPTKTWLALVRIFSGRHPMLFSYQRSLPRQPVPSVQ
DTVRKYLESVRPILSDEDFDWTAVLAQEFLRLQASLLQWYLRLKSWWASNYVSDWWEEFV
YLRSRNPLMVNSNYYMMDFLYVTPTPLQAARAGNAVHALLLYRHRLNRQEIPPTLLMGMR
PLCSAQYEKIFNTTRIPGVQKDYIRHLHDSQHVAVFHRGRFFRMGTHSRNSLLSPRALEQ
QFQRILDDPSPACPHEEHLAALTAAPRGTWAQVRTSLKTQAAEALEAVEGAAFFVSLDAE
PAGLTREDPAASLDAYAHALLAGRGHDRWFDKSFTLIVFSNGKLGLSVEHSWADCPISGH
MWEFTLATECFQLGYSTDGHCKGHPDPTLPQPQRLQWDLPDQIHSSISLALRGAKILSEN
VDCHVVPFSLFGKSFIRRCHLSSDSFIQIALQLAHFRDRGQFCLTYESAMTRLFLEGRTE
TVRSCTREACNFVRAMEDKEKTDPQCLALFRVAVDKHQALLKAAMSGQGVDRHLFALYIV
SRFLHLQSPFLTQVHSEQWQLSTSQIPVQQMHLFDVHNYPDYVSSGGGFGPADDHGYGVS
YIFMGDGMITFHISSKKSSTKTDSHRLGQHIEDALLDVASLFQAGQHFKRRFRGSGKENS
RHRCGFLSRQTGASKASMTSTDF
Enzyme 4 Number of Residues 803
Enzyme 4 Molecular Weight 90990
Enzyme 4 Theoretical pI 8.18
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 Not Available
Enzyme 4 Pathways Not Available
Enzyme 4 Reactions Not Available
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • 1-74
Enzyme 4 Transmembrane Regions
  • 53-75
  • 104-126
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 33340613 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID Q5K6N5 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name Q5K6N5_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >2412 bp 
ATGGCTGAAGCGCACCAGGCCGTGGGCTTCCGACCCTCGCTGACCTCGGACGGGGCTGAA
GTGGAACTCAGTGCCCCTGTGCTGCAGGAGATCTACCTCTCTGGCCTGCGCTCCTGGAAA
AGGCATCTCTCACGTTTCTGGAATGACTTTCTCACCGGTGTGTTTCCTGCCAGCCCCCTC
AGTTGGCTTTTCCTCTTCAGTGCCATCCAGCTTGCCTGGTTCCTCCAGCTGGATCCTTCC
TTAGGACTGATGGAGAAGATCAAAGAGTTGCTGCCTGACTGGGGTGGACAACACCACGGG
CTCCGGGGGGTCCTGGCAGCCGCGCTGTTTGCCTCGTGTTTGTGGGGAGCCCTGATCTTC
ACACTGCACGTGGCCCTGAGGCTGCTTCTGTCCTACCACGGCTGGCTTCTTGAGCCCCAC
GGAGCCATGTCCTCCCCCACCAAGACCTGGCTGGCCCTGGTCCGCATCTTCTCTGGCCGC
CACCCGATGCTGTTCAGTTACCAGCGCTCCCTGCCACGCCAGCCCGTGCCCTCTGTGCAG
GACACCGTGCGCAAGTACCTGGAGTCGGTCCGGCCCATCCTCTCCGACGAGGACTTCGAC
TGGACCGCGGTCCTGGCGCAGGAATTCCTGAGGCTGCAGGCGTCGCTGCTGCAGTGGTAC
CTGCGGCTCAAGTCCTGGTGGGCGTCCAATTATGTCAGTGACTGGTGGGAGGAATTTGTG
TACCTGCGCTCCCGAAATCCGCTGATGGTGAACAGCAACTATTACATGATGGACTTCCTG
TATGTCACACCCACGCCTCTGCAGGCAGCTCGCGCTGGGAATGCCGTCCATGCCCTCCTC
CTGTACCGCCACCGCCTGAACCGCCAGGAGATACCCCCGACTTTGCTGATGGGAATGCGC
CCCTTATGCTCTGCCCAGTACGAGAAGATCTTCAACACCACGCGGATTCCAGGGGTCCAA
AAAGACTACATCCGCCACCTCCATGACAGCCAACACGTGGCTGTCTTCCACCGGGGCCGA
TTCTTCCGCATGGGGACCCACTCCCGAAACAGCCTGCTTTCCCCGAGAGCCCTGGAGCAG
CAGTTTCAGAGAATCCTGGATGATCCCTCACCGGCCTGCCCCCACGAGGAACATCTGGCA
GCTCTGACAGCTGCTCCCAGGGGCACGTGGGCCCAGGTGCGGACATCCCTGAAGACCCAG
GCAGCGGAGGCCCTGGAGGCGGTGGAAGGGGCCGCTTTCTTTGTGTCACTGGATGCTGAG
CCCGCGGGGCTCACCAGGGAGGACCCGGCAGCGTCGTTGGATGCCTACGCCCATGCTCTG
CTGGCCGGCCGGGGCCATGATCGCTGGTTTGACAAATCCTTCACCCTAATCGTCTTCTCT
AACGGGAAGCTGGGCCTCAGCGTGGAGCACTCCTGGGCCGACTGCCCCATCTCAGGACAC
ATGTGGGAGTTCACTCTGGCTACAGAATGCTTTCAGCTGGGCTACTCAACAGACGGCCAC
TGCAAGGGGCACCCGGACCCCACACTACCCCAGCCCCAGCGGCTGCAATGGGACCTTCCA
GACCAGATCCACTCCTCCATCTCTCTAGCCCTGAGGGGAGCCAAGATCTTGTCTGAAAAT
GTCGACTGCCATGTCGTTCCATTCTCCCTATTTGGCAAGAGCTTCATCCGACGCTGCCAC
CTCTCTTCAGACAGCTTCATCCAGATCGCCTTGCAACTGGCCCACTTCCGGGACAGGGGT
CAATTCTGCCTGACTTATGAGTCGGCCATGACTCGCTTATTCCTGGAAGGCCGGACGGAG
ACGGTGCGGTCTTGCACGAGGGAGGCCTGCAACTTTGTCAGGGCCATGGAGGACAAAGAG
AAGACGGACCCACAGTGCCTCGCCCTGTTCCGCGTGGCAGTGGACAAGCACCAGGCTCTG
CTGAAGGCAGCCATGAGCGGGCAGGGAGTTGACCGCCACCTGTTTGCGCTGTACATCGTG
TCCCGATTCCTCCACCTGCAGTCGCCCTTCCTGACCCAGGTCCATTCGGAGCAGTGGCAG
CTGTCCACCAGCCAGATCCCTGTTCAGCAAATGCATCTGTTTGACGTCCACAATTACCCG
GACTATGTTTCCTCAGGCGGTGGATTCGGGCCTGCTGATGACCATGGTTATGGTGTTTCT
TATATCTTCATGGGGGATGGCATGATCACCTTCCACATCTCCAGCAAAAAATCAAGCACA
AAAACGGATTCCCACAGGCTGGGGCAGCACATTGAGGACGCACTGCTGGATGTGGCCTCC
CTGTTCCAGGCGGGACAGCATTTTAAGCGCCGGTTCAGAGGGTCAGGGAAGGAGAACTCC
AGGCACAGGTGTGGATTTCTCTCCCGCCAGACTGGGGCCTCCAAGGCCTCAATGACATCC
ACCGACTTCTGA
Enzyme 4 GenBank Gene ID AF331918 Link Image
Enzyme 4 GeneCard ID CATL1 Link Image
Enzyme 4 GenAtlas ID CATL1 Link Image
Enzyme 4 HGNC ID HGNC:18540 Link Image
Enzyme 4 Chromosome Location Not Available
Enzyme 4 Locus Not Available
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References Not Available
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 16472
Enzyme 5 Name cDNA, FLJ93082, Homo sapiens carnitine palmitoyltransferase II (CPT2), nuclear geneencoding mitochondrial protein, mRNA (Carnitine palmitoyltransferase II)
Enzyme 5 Synonyms Not Available
Enzyme 5 Gene Name CPT2
Enzyme 5 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 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 Not Available
Enzyme 5 Pathways Not Available
Enzyme 5 Reactions Not Available
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein Not Available
Enzyme 5 UniProtKB/Swiss-Prot ID B2R6S0 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name B2R6S0_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence Not Available
Enzyme 5 GenBank Gene ID AK312687 Link Image
Enzyme 5 GeneCard ID B2R6S0 Link Image
Enzyme 5 GenAtlas ID Not Available
Enzyme 5 HGNC ID Not Available
Enzyme 5 Chromosome Location Not Available
Enzyme 5 Locus Not Available
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References Not Available
Enzyme 5 Metabolite References Not Available