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Human Metabolome Database Version 2.5

 

Showing metabocard for Dodecanoic acid (HMDB00638)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-05-05 20:58:07
Accession Number HMDB00638
Secondary Accession Numbers Not Available
Common Name Dodecanoic acid
Description Lauric acid, or dodecanoic acid is the main fatty acid in coconut oil and in palm kernel oil, and is believed to have antimicrobial properties. It is a white, powdery solid with a faint odor of bay oil. Lauric acid, although slightly irritating to mucous membranes, has a very low toxicity and so is used in many soaps and shampoos.
Synonyms
  1. 1-Undecanecarboxylate
  2. 1-Undecanecarboxylic acid
  3. ABL
  4. Aliphat No. 4
  5. Dodecanoate
  6. Dodecylate
  7. Dodecylic acid
  8. Edenor C 1298-100
  9. Emery 651
  10. Hystrene 9512
  11. Kortacid 1299
  12. Laurate
  13. Lauric acid
  14. Laurostearate
  15. Laurostearic acid
  16. Lunac L 70
  17. Lunac L 98
  18. Neo-Fat 12
  19. Neo-Fat 12-43
  20. Nissan NAA 122
  21. Philacid 1200
  22. Prifac 2920
  23. Univol U 314
  24. Vulvate
  25. Vulvic acid
  26. n-Dodecanoate
  27. n-Dodecanoic acid
  28. Dodecanoic acid
Chemical IUPAC Name Dodecanoic acid
Chemical Formula C12H24O2
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Organic acids
Class
  • Fatty Acids
Sub Class
  • Medium chain fatty acids
Family
  • Mammalian Metabolite
Species
  • carboxylic acid
Biofunction
—
Application
—
Source
  • Endogenous
Average Molecular Weight 200.318
Monoisotopic Molecular Weight 200.177628
Isomeric SMILES CCCCCCCCCCCC(O)=O
Canonical SMILES CCCCCCCCCCCC(O)=O
KEGG Compound ID C02679 Link Image
BioCyc ID Not Available
BiGG ID 40351 Link Image
Wikipedia Link Dodecanoic acid Link Image
NuGOwiki Link HMDB00638 Link Image
Metagene Link HMDB00638 Link Image
METLIN ID 5611 Link Image
PubChem Compound 3893 Link Image
PubChem Substance 7990961 Link Image
ChEBI ID 18262 Link Image
CAS Registry Number 143-07-7
InChI Identifier InChI=1/C12H24O2/c1-2-3-4-5-6-7-8-9-10-11-12(13)14/h2-11H2,1H3,(H,13,14)
Synthesis Reference Stepanova, G. A.; Markevich, V. S.; Garanin, V. I.; Stychinskii, G. F. Synthesis of lauric acid. Khimicheskaya Promyshlennost (Moscow, Russian Federation) (1974), (12), 930.
Melting Point (Experimental) 44-46 oC
Experimental Water Solubility 0.00481 mg/mL [YALKOWSKY,SH & DANNENFELSER,RM (1992)] Source: PhysProp
Predicted Water Solubility 9.97e-03 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -1
State Liquid
Experimental LogP/Hydrophobicity 4.60 [SANGSTER (1993)] Source: PhysProp
Predicted LogP/Hydrophobicity 5.13 [Predicted by ALOGPS]; 5.3 [Predicted by PubChem via XLOGP] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID 1E7F 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 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
  • Membrane (Predicted from LogP)
  • Cytoplasm
Biofluid Location
  • Blood
  • Cerebrospinal Fluid
  • Urine
Tissue Location
Tissue References
Liver —
Stratum Corneum —
Thyroid Gland —
Concentrations (Normal)
Biofluid Blood
Value 12.0 (2.0-37.0) uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Hoffmann GF, Meier-Augenstein W, Stockler S, Surtees R, Rating D, Nyhan WL: Physiology and pathophysiology of organic acids in cerebrospinal fluid. J Inherit Metab Dis. 1993;16(4):648-69. [PubMed Link Image]
Biofluid CSF
Value 2.8 +/- 2.8 uM
Age Adult:>18 yrs old
Sex N/A
Patient information Normal
Comments Not Available
References
  • Hoffmann GF, Meier-Augenstein W, Stockler S, Surtees R, Rating D, Nyhan WL: Physiology and pathophysiology of organic acids in cerebrospinal fluid. J Inherit Metab Dis. 1993;16(4):648-69. [PubMed Link Image]
Biofluid Urine
Value 0.03 +/- 0.02 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 130. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp. Basel, Switzerland c1981-1992.
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Beta Oxidation of Very Long Chain Fatty Acids SMP00052 Link Image map01040 Link Image
Fatty Acid Biosynthesis SMP00456 Link Image
Mitochondrial Beta-Oxidation of Medium Chain Saturated Fatty Acids SMP00481 Link Image
General References
  1. Amet Y, Berthou F, Fournier G, Dreano Y, Bardou L, Cledes J, Menez JF: Cytochrome P450 4A and 2E1 expression in human kidney microsomes. Biochem Pharmacol. 1997 Mar 21;53(6):765-71. [PubMed Link Image]
  2. Smith SW, Anderson BD: Human skin permeability enhancement by lauric acid under equilibrium aqueous conditions. J Pharm Sci. 1995 May;84(5):551-6. [PubMed Link Image]
  3. Powell PK, Wolf I, Lasker JM: Identification of CYP4A11 as the major lauric acid omega-hydroxylase in human liver microsomes. Arch Biochem Biophys. 1996 Nov 1;335(1):219-26. [PubMed Link Image]
  4. Ryan MT, Chopra RK: The paradoxical effect of fatty acid on steroid-albumin interaction. Biochim Biophys Acta. 1976 Mar 18;427(1):337-49. [PubMed Link Image]
  5. Amet Y, Berthou F, Baird S, Dreano Y, Bail JP, Menez JF: Validation of the (omega-1)-hydroxylation of lauric acid as an in vitro substrate probe for human liver CYP2E1. Biochem Pharmacol. 1995 Nov 27;50(11):1775-82. [PubMed Link Image]
  6. Kitahara T, Koyama N, Matsuda J, Aoyama Y, Hirakata Y, Kamihira S, Kohno S, Nakashima M, Sasaki H: Antimicrobial activity of saturated fatty acids and fatty amines against methicillin-resistant Staphylococcus aureus. Biol Pharm Bull. 2004 Sep;27(9):1321-6. [PubMed Link Image]
  7. NTP Toxicology and Carcinogenesis Studies of Lauric Acid Diethanolamine Condensate (CAS NO. 120-40-1) in F344/N Rats and B6C3F1 Mice (Dermal Studies). Natl Toxicol Program Tech Rep Ser. 1999 Jul;480:1-200. [PubMed Link Image]
  8. Hoffmann GF, Meier-Augenstein W, Stockler S, Surtees R, Rating D, Nyhan WL: Physiology and pathophysiology of organic acids in cerebrospinal fluid. J Inherit Metab Dis. 1993;16(4):648-69. [PubMed Link Image]
  9. Amet Y, Berthou F, Menez JF: Simultaneous radiometric and fluorimetric detection of lauric acid metabolites using high-performance liquid chromatography following esterification with 4-bromomethyl-6,7-dimethoxycoumarin in human and rat liver microsomes. J Chromatogr B Biomed Appl. 1996 Jun 7;681(2):233-9. [PubMed Link Image]
  10. Wikipedia Link Image
Metabolic Enzymes
  1. Peroxisomal carnitine O-octanoyltransferase
  2. Carnitine O-palmitoyltransferase 2, mitochondrial precursor
  3. Mitochondrial carnitine/acylcarnitine carrier protein
  4. Thioesterase domain containing 1
Enzyme 1 [top]
Enzyme 1 ID 5542
Enzyme 1 Name Peroxisomal carnitine O-octanoyltransferase
Enzyme 1 Synonyms
  1. COT
Enzyme 1 Gene Name CROT
Enzyme 1 Protein Sequence >Peroxisomal carnitine O-octanoyltransferase 
MENQLAKSTEERTFQYQDSLPSLPVPSLEESLKKYLESVKPFANQEEYKKTEEIVQKFQS
GIGEKLHQKLLERAKGKRNWLEEWWLNVAYLDVRIPSQLNVNFAGPAAHFEHYWPPKEGT
QLERGSITLWHNLNYWQLLRKEKVPVHKVGNTPLDMNQFRMLFSTCKVPGITRDSIMNYF
RTESEGRSPNHIVVLCRGRAFVFDVIHEGCLVTPPELLRQLTYIHKKCHSEPDGPGIAAL
TSEERTRWAKAREYLIGLDPENLALLEKIQSSLLVYSMEDSSPHVTPEDYSEIIAAILIG
DPTVRWGDKSYNLISFSNGVFGCNCDHAPFDAMIMVNISYYVDEKIFQNEGRWKGSEKVR
DIPLPEELIFIVDEKVLNDINQAKAQYLREASDLQIAAYAFTSFGKKLTKNKMLHPDTFI
QLALQLAYYRLHGHPGCCYETAMTRHFYHGRTETMRSCTVEAVRWCQSMQDPSVNLRERQ
QKMLQAFAKHNKMMKDCSAGKGFDRHLLGLLLIAKEEGLPVPELFTDPLFSKSGGGGNFV
LSTSLVGYLRVQGVVVPMVHNGYGFFYHIRDDRFVVACSAWKSCPETDAEKLVQLTFCAF
HDMIQLMNSTHL
Enzyme 1 Number of Residues 612
Enzyme 1 Molecular Weight 70179
Enzyme 1 Theoretical pI 7.09
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 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 1 Pathways Not Available
Enzyme 1 Reactions
  • octanoyl-CoA + L-carnitine = CoA + L-octanoylcarnitine
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 6066280 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID Q9UKG9 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name OCTC_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 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 1 GenBank Gene ID AF168793 Link Image
Enzyme 1 GeneCard ID CROT Link Image
Enzyme 1 GenAtlas ID CROT Link Image
Enzyme 1 HGNC ID HGNC:2366 Link Image
Enzyme 1 Chromosome Location 7
Enzyme 1 Locus 7q21.1
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 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 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5546
Enzyme 2 Name Carnitine O-palmitoyltransferase 2, mitochondrial precursor
Enzyme 2 Synonyms
  1. Carnitine palmitoyltransferase II
  2. CPT II
Enzyme 2 Gene Name CPT2
Enzyme 2 Protein Sequence >Carnitine O-palmitoyltransferase 2, mitochondrial precursor 
MVPRLLLRAWPRGPAVGPGAPSRPLSAGSGPGQYLQRSIVPTMHYQDSLPRLPIPKLEDT
IRRYLSAQKPLLNDGQFRKTEQFCKSFENGIGKELHEQLVALDKQNKHTSYISGPWFDMY
LSARDSVVLNFNPFMAFNPDPKSEYNDQLTRATNMTVSAIRFLKTLRAGLLEPEVFHLNP
AKSDTITFKRLIRFVPSSLSWYGAYLVNAYPLDMSQYFRLFNSTRLPKPSRDELFTDDKA
RHLLVLRKGNFYIFDVLDQDGNIVSPSEIQAHLKYILSDSSPAPEFPLAYLTSENRDIWA
ELRQKLMSSGNEESLRKVDSAVFCLCLDDFPIKDLVHLSHNMLHGDGTNRWFDKSFNLII
AKDGSTAVHFEHSWGDGVAVLRFFNEVFKDSTQTPAVTPQSQPATTDSTVTVQKLNFELT
DALKTGITAAKEKFDATMKTLTIDCVQFQRGGKEFLKKQKLSPDAVAQLAFQMAFLRQYG
QTVATYESCSTAAFKHGRTETIRPASVYTKRCSEAFVREPSRHSAGELQQMMVECSKYHG
QLTKEAAMGQGFDRHLFALRHLAAAKGIILPELYLDPAYGQINHNVLSTSTLSSPAVNLG
GFAPVVSDGFGVGYAVHDNWIGCNVSSYPGRNAREFLQCVEKALEDMFDALEGKSIKS
Enzyme 2 Number of Residues 658
Enzyme 2 Molecular Weight 73778
Enzyme 2 Theoretical pI 8.30
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
  • 1-15
Enzyme 2 Transmembrane Regions Not Available
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 1041195 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P23786 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name CPT2_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 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 2 GenBank Gene ID U09648 Link Image
Enzyme 2 GeneCard ID CPT2 Link Image
Enzyme 2 GenAtlas ID CPT2 Link Image
Enzyme 2 HGNC ID HGNC:2330 Link Image
Enzyme 2 Chromosome Location 1
Enzyme 2 Locus 1p32
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 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 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 8300
Enzyme 3 Name Mitochondrial carnitine/acylcarnitine carrier protein
Enzyme 3 Synonyms
  1. Carnitine/acylcarnitine translocase
  2. CAC
  3. Solute carrier family 25 member 20
Enzyme 3 Gene Name SLC25A20
Enzyme 3 Protein Sequence >Mitochondrial carnitine/acylcarnitine carrier protein 
MADQPKPISPLKNLLAGGFGGVCLVFVGHPLDTVKVRLQTQPPSLPGQPPMYSGTFDCFR
KTLFREGITGLYRGMAAPIIGVTPMFAVCFFGFGLGKKLQQKHPEDVLSYPQLFAAGMLS
GVFTTGIMTPGERIKCLLQIQASSGESKYTGTLDCAKKLYQEFGIRGIYKGTVLTLMRDV
PASGMYFMTYEWLKNIFTPEGKRVSELSAPRILVAGGIAGIFNWAVAIPPDVLKSRFQTA
PPGKYPNGFRDVLRELIRDEGVTSLYKGFNAVMIRAFPANAACFLGFEVAMKFLNWATPN
L
Enzyme 3 Number of Residues 301
Enzyme 3 Molecular Weight 32944
Enzyme 3 Theoretical pI 9.84
Enzyme 3 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 3 General Function Not Available
Enzyme 3 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 3 Pathways Not Available
Enzyme 3 Reactions Not Available
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • 13-31 74-93 113-131 171-190 212-230 268-287
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 2765075 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID O43772 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name MCAT_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >906 bp 
ATGGCCGACCAGCCAAAACCCATCAGCCCGCTCAAGAACCTGCTGGCCGGCGGCTTTGGC
GGCGTGTGCCTGGTGTTCGTCGGTCACCCTCTGGACACGGTCAAGGTCCGACTGCAGACA
CAGCCACCGAGTTTGCCTGGACAACCTCCCATGTACTCTGGGACCTTTGACTGTTTCCGG
AAGACTCTTTTTAGAGAGGGCATCACGGGGCTATATCGGGGAATGGCTGCCCCTATCATC
GGGGTCACTCCCATGTTTGCCGTGTGCTTCTTTGGGTTTGGTTTGGGGAAGAAACTACAA
CAGAAACACCCAGAAGATGTGCTCAGCTATCCCCAGCTTTTTGCAGCTGGGATGTTATCT
GGCGTATTCACCACAGGAATCATGACTCCTGGAGAACGGATCAAGTGCTTATTACAGATT
CAGGCTTCTTCAGGAGAAAGCAAGTACACTGGTACCTTGGACTGTGCAAAGAAGCTGTAC
CAGGAGTTTGGGATCCGAGGCATCTACAAAGGGACTGTGCTTACCCTTATGCGAGATGTC
CCAGCTAGTGGAATGTATTTCATGACATATGAATGGCTGAAAAATATCTTCACTCCGGAG
GGAAAGAGGGTCAGTGAGCTCAGTGCCCCTCGGATCTTGGTGGCTGGGGGCATTGCAGGG
ATCTTCAACTGGGCTGTGGCAATCCCCCCAGATGTGCTCAAGTCTCGATTCCAGACTGCA
CCTCCTGGGAAATATCCTAATGGTTTCAGAGATGTGCTGAGGGAGCTGATCCGGGATGAA
GGAGTCACATCCTTGTACAAAGGGTTCAATGCAGTGATGATCCGAGCCTTCCCAGCCAAT
GCGGCCTGTTTCCTTGGCTTTGAAGTTGCCATGAAGTTCCTTAATTGGGCCACCCCCAAC
TTGTGA
Enzyme 3 GenBank Gene ID Y10319 Link Image
Enzyme 3 GeneCard ID SLC25A20 Link Image
Enzyme 3 GenAtlas ID SLC25A20 Link Image
Enzyme 3 HGNC ID HGNC:1421 Link Image
Enzyme 3 Chromosome Location 3
Enzyme 3 Locus 3p21.31
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 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 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 8493
Enzyme 4 Name Thioesterase domain containing 1
Enzyme 4 Synonyms Not Available
Enzyme 4 Gene Name THEDC1
Enzyme 4 Protein Sequence >Thioesterase domain containing 1 
MERGDQPKRTRNENIFNCLYKNPEATFKLICFPWMGGGSTHFAKWGQDTHDLLEVHSLRL
PGRESRVEEPLENDISQLVDEVVCALQPVIQDKPFAFFGHSMGSYIAFRTALGLKENNQP
EPLHLFLSSATPVHSKAWHRIPKDDELSEEQISHYLMEFGGTPKHFAEAKEFVKQCSPII
RADLNIVRSCTSNVPSKAVLSCDLTCFVGSEDIAKDMEAWKDVTSGNAKIYQLPGGHFYL
LDPANEKLIKNYIIKCLEVSSISNF
Enzyme 4 Number of Residues 265
Enzyme 4 Molecular Weight 29931
Enzyme 4 Theoretical pI 6.17
Enzyme 4 GO Classification
Function
  • CoA hydrolase activity
  • acyl-CoA thioesterase II activity
  • acyl-CoA thioesterase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • thiolester hydrolase activity
Process
  • biosynthesis
  • metabolism
  • physiological process
Component
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Enzyme 4 General Function Secondary metabolites biosynthesis, transport and catabolism
Enzyme 4 Specific Function Not Available
Enzyme 4 Pathways Not Available
Enzyme 4 Reactions Not Available
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals Not Available
Enzyme 4 Transmembrane Regions Not Available
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein Not Available
Enzyme 4 UniProtKB/Swiss-Prot ID Q5VUB6 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name Q5VUB6_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence Not Available
Enzyme 4 GenBank Gene ID AL590365 Link Image
Enzyme 4 GeneCard ID OLAH Link Image
Enzyme 4 GenAtlas ID OLAH Link Image
Enzyme 4 HGNC ID HGNC:25625 Link Image
Enzyme 4 Chromosome Location 10
Enzyme 4 Locus 10p13
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References Not Available
Enzyme 4 Metabolite References Not Available