The Enzyme Database

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EC 1.3.8.13     
Accepted name: crotonobetainyl-CoA reductase
Reaction: γ-butyrobetainyl-CoA + electron-transfer flavoprotein = crotonobetainyl-CoA + reduced electron-transfer flavoprotein
Glossary: γ-butyrobetainyl-CoA = 4-(trimethylammonio)butanoyl-CoA
crotonobetainyl-CoA = (E)-4-(trimethylammonio)but-2-enoyl-CoA
Other name(s): caiA (gene name)
Systematic name: γ-butyrobetainyl-CoA:electron-transfer flavoprotein 2,3-oxidoreductase
Comments: The enzyme has been purified from the bacterium Escherichia coli O44 K74, in which it forms a complex with EC 2.8.3.21, L-carnitine CoA-transferase. The electron donor is believed to be an electron-transfer flavoprotein (ETF) encoded by the fixA and fixB genes.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Roth, S., Jung, K., Jung, H., Hommel, R.K. and Kleber, H.P. Crotonobetaine reductase from Escherichia coli - a new inducible enzyme of anaerobic metabolization of L(–)-carnitine. Antonie Van Leeuwenhoek 65 (1994) 63–69. [PMID: 8060125]
2.  Preusser, A., Wagner, U., Elssner, T. and Kleber, H.P. Crotonobetaine reductase from Escherichia coli consists of two proteins. Biochim. Biophys. Acta 1431 (1999) 166–178. [DOI] [PMID: 10209289]
3.  Elssner, T., Hennig, L., Frauendorf, H., Haferburg, D. and Kleber, H.P. Isolation, identification, and synthesis of γ-butyrobetainyl-CoA and crotonobetainyl-CoA, compounds involved in carnitine metabolism of E. coli. Biochemistry 39 (2000) 10761–10769. [DOI] [PMID: 10978161]
4.  Walt, A. and Kahn, M.L. The fixA and fixB genes are necessary for anaerobic carnitine reduction in Escherichia coli. J. Bacteriol. 184 (2002) 4044–4047. [DOI] [PMID: 12081978]
[EC 1.3.8.13 created 2017]
 
 
EC 1.14.13.239     
Accepted name: carnitine monooxygenase
Reaction: L-carnitine + NAD(P)H + H+ + O2 = (3R)-3-hydroxy-4-oxobutanoate + trimethylamine + NAD(P)+ + H2O
Glossary: (3R)-3-hydroxy-4-oxobutanoate = L-malic semialdehyde
Other name(s): cntAB (gene names); yeaWX (gene names)
Systematic name: L-carnitine,NAD(P)H:oxygen oxidoreductase (trimethylamine-forming)
Comments: The bacterial enzyme is a complex consisting of a reductase and an oxygenase components. The reductase subunit contains a flavin and a plant-type ferredoxin [2Fe-2S] cluster, while the oxygenase subunit is a Rieske-type protein in which a [2Fe-2S] cluster is coordinated by two histidine and two cysteine residues.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Ditullio, D., Anderson, D., Chen, C.S. and Sih, C.J. L-Carnitine via enzyme-catalyzed oxidative kinetic resolution. Bioorg. Med. Chem. 2 (1994) 415–420. [DOI] [PMID: 8000862]
2.  Zhu, Y., Jameson, E., Crosatti, M., Schafer, H., Rajakumar, K., Bugg, T.D. and Chen, Y. Carnitine metabolism to trimethylamine by an unusual Rieske-type oxygenase from human microbiota. Proc. Natl. Acad. Sci. USA 111 (2014) 4268–4273. [DOI] [PMID: 24591617]
3.  Koeth, R.A., Levison, B.S., Culley, M.K., Buffa, J.A., Wang, Z., Gregory, J.C., Org, E., Wu, Y., Li, L., Smith, J.D., Tang, W.H., DiDonato, J.A., Lusis, A.J. and Hazen, S.L. γ-Butyrobetaine is a proatherogenic intermediate in gut microbial metabolism of L-carnitine to TMAO. Cell Metab 20 (2014) 799–812. [DOI] [PMID: 25440057]
[EC 1.14.13.239 created 2017]
 
 
EC 2.3.1.21     
Accepted name: carnitine O-palmitoyltransferase
Reaction: palmitoyl-CoA + L-carnitine = CoA + L-palmitoylcarnitine
Other name(s): CPT (ambiguous); CPTo; outer malonyl-CoA inhibitable carnitine palmitoyltransferase; CPTi; CPT I (outer membrane carnitine palmitoyl transferase); carnitine palmitoyltransferase I; carnitine palmitoyltransferase II; CPT-A; CPT-B; acylcarnitine transferase; carnitine palmitoyltransferase; carnitine palmitoyltransferase-A; L-carnitine palmitoyltransferase; palmitoylcarnitine transferase
Systematic name: palmitoyl-CoA:L-carnitine O-palmitoyltransferase
Comments: Broad specificity to acyl group, over the range C8 to C18; optimal activity with palmitoyl-CoA. cf. EC 2.3.1.7 carnitine O-acetyltransferase and EC 2.3.1.137 carnitine O-octanoyltransferase.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9068-41-1
References:
1.  Derrick, J.P., Tubbs, P.K. and Ramsay, R.R. Purification and properties of an easily solubilized L-carnitine palmitoyltransferase from beef-liver mitochondria. Biochem. Soc. Trans. 14 (1986) 698.
2.  Healy, M.J., Kerner, J. and Bieber, L.L. Enzymes of carnitine acylation. Is overt carnitine palmitoyltransferase of liver peroxisomal carnitine octanoyltransferase? Biochem. J. 249 (1988) 231–237. [PMID: 3342008]
3.  Miyazawa, S., Ozasa, H., Osumi, T. and Hashimoto, T. Purification and properties of carnitine octanoyltransferase and carnitine palmitoyltransferase from rat liver. J. Biochem. (Tokyo) 94 (1983) 529–542. [PMID: 6630173]
[EC 2.3.1.21 created 1972]
 
 
EC 2.3.1.137     
Accepted name: carnitine O-octanoyltransferase
Reaction: octanoyl-CoA + L-carnitine = CoA + L-octanoylcarnitine
Other name(s): medium-chain/long-chain carnitine acyltransferase; carnitine medium-chain acyltransferase; easily solubilized mitochondrial carnitine palmitoyltransferase; overt mitochondrial carnitine palmitoyltransferase
Systematic name: octanoyl-CoA:L-carnitine O-octanoyltransferase
Comments: Acts on a range of acyl-CoAs, with optimal activity with C6 or C8 acyl groups. cf. EC 2.3.1.7 (carnitine O-acetyltransferase) and EC 2.3.1.21 (carnitine O-palmitoyltransferase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 39369-19-2
References:
1.  Farrell, S.O., Fiol, C.J., Reddy, J.K. and Bieber, L.L. Properties of purified carnitine acyltransferases of mouse liver peroxisomes. J. Biol. Chem. 259 (1984) 13089–13095. [PMID: 6436243]
2.  Healy, M.J., Kerner, J. and Bieber, L.L. Enzymes of carnitine acylation. Is overt carnitine palmitoyltransferase of liver peroxisomal carnitine octanoyltransferase? Biochem. J. 249 (1988) 231–237. [PMID: 3342008]
3.  Miyazawa, S., Ozasa, H., Osumi, T. and Hashimoto, T. Purification and properties of carnitine octanoyltransferase and carnitine palmitoyltransferase from rat liver. J. Biochem. (Tokyo) 94 (1983) 529–542. [PMID: 6630173]
[EC 2.3.1.137 created 1992]
 
 
EC 2.8.3.21     
Accepted name: L-carnitine CoA-transferase
Reaction: (1) (E)-4-(trimethylammonio)but-2-enoyl-CoA + L-carnitine = (E)-4-(trimethylammonio)but-2-enoate + L-carnitinyl-CoA
(2) 4-trimethylammoniobutanoyl-CoA + L-carnitine = 4-trimethylammoniobutanoate + L-carnitinyl-CoA
Glossary: L-carnitine = (3R)-3-hydroxy-4-(trimethylammonio)butanoate
(E)-4-(trimethylammonio)but-2-enoate = crotonobetaine
4-trimethylammoniobutanoate = γ-butyrobetaine
Other name(s): CaiB; crotonobetainyl/γ-butyrobetainyl-CoA:carnitine CoA-transferase
Systematic name: (E)-4-(trimethylammonio)but-2-enoyl-CoA:L-carnitine CoA-transferase
Comments: The enzyme is found in gammaproteobacteria such as Proteus sp. and Escherichia coli. It has similar activity with both substrates.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Engemann, C., Elssner, T. and Kleber, H.P. Biotransformation of crotonobetaine to L-(–)-carnitine in Proteus sp. Arch. Microbiol. 175 (2001) 353–359. [PMID: 11409545]
2.  Elssner, T., Engemann, C., Baumgart, K. and Kleber, H.P. Involvement of coenzyme A esters and two new enzymes, an enoyl-CoA hydratase and a CoA-transferase, in the hydration of crotonobetaine to L-carnitine by Escherichia coli. Biochemistry 40 (2001) 11140–11148. [DOI] [PMID: 11551212]
3.  Stenmark, P., Gurmu, D. and Nordlund, P. Crystal structure of CaiB, a type-III CoA transferase in carnitine metabolism. Biochemistry 43 (2004) 13996–14003. [DOI] [PMID: 15518548]
4.  Engemann, C., Elssner, T., Pfeifer, S., Krumbholz, C., Maier, T. and Kleber, H.P. Identification and functional characterisation of genes and corresponding enzymes involved in carnitine metabolism of Proteus sp. Arch. Microbiol. 183 (2005) 176–189. [DOI] [PMID: 15731894]
5.  Rangarajan, E.S., Li, Y., Iannuzzi, P., Cygler, M. and Matte, A. Crystal structure of Escherichia coli crotonobetainyl-CoA: carnitine CoA-transferase (CaiB) and its complexes with CoA and carnitinyl-CoA. Biochemistry 44 (2005) 5728–5738. [DOI] [PMID: 15823031]
[EC 2.8.3.21 created 2014]
 
 
EC 3.1.1.28     
Accepted name: acylcarnitine hydrolase
Reaction: O-acylcarnitine + H2O = a fatty acid + L-carnitine
Other name(s): high activity acylcarnitine hydrolase; HACH; carnitine ester hydrolase; palmitoylcarnitine hydrolase; palmitoyl-L-carnitine hydrolase; long-chain acyl-L-carnitine hydrolase; palmitoyl carnitine hydrolase
Systematic name: O-acylcarnitine acylhydrolase
Comments: Acts on higher fatty acid (C6 to C18) esters of L-carnitine; highest activity is with O-decanoyl-L-carnitine.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37278-42-5
References:
1.  Mahadevan, S. and Sauer, F. Carnitine ester hydrolase of rat liver. J. Biol. Chem. 244 (1969) 4448–4453. [PMID: 5806585]
2.  Mentlein, R., Reuter, G. and Heymann, E. Specificity of two different purified acylcarnitine hydrolases from rat liver, their identity with other carboxylesterases, and their possible function. Arch. Biochem. Biophys. 240 (1985) 801–810. [DOI] [PMID: 4026306]
[EC 3.1.1.28 created 1972]
 
 
EC 3.5.1.73     
Accepted name: carnitinamidase
Reaction: L-carnitinamide + H2O = L-carnitine + NH3
Other name(s): L-carnitinamidase; carnitine amidase; L-carnitine amidase
Systematic name: L-carnitinamide amidohydrolase
Comments: Does not act on D-carnitinamide.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 117444-04-9
References:
1.  Nakayama, K., Honda, H., Ogawa, Y., Ozawa, T. and Ota, T. Method for producing carnitine, L- carnitinamide hydrolase and method for producing same. Patent DE3728321, Chem. Abstr. (1988), 109, 22873.
[EC 3.5.1.73 created 1992]
 
 
EC 4.2.1.89      
Deleted entry: carnitine dehydratase. The activity has now been shown to be due to EC 2.8.3.21, L-carnitine CoA-transferase and EC 4.2.1.149, crotonobetainyl-CoA hydratase.
[EC 4.2.1.89 created 1989, deleted 2014]
 
 
EC 4.2.1.149     
Accepted name: crotonobetainyl-CoA hydratase
Reaction: L-carnitinyl-CoA = (E)-4-(trimethylammonio)but-2-enoyl-CoA + H2O
Glossary: L-carnitinyl-CoA = (3R)-3-hydroxy-4-(trimethylammonio)butanoyl-CoA
(E)-4-(trimethylammonio)but-2-enoyl-CoA = crotonobetainyl-CoA
Other name(s): CaiD; L-carnityl-CoA dehydratase
Systematic name: L-carnitinyl-CoA hydro-lyase [(E)-4-(trimethylammonio)but-2-enoyl-CoA-forming]
Comments: The enzyme is also able to use crotonyl-CoA as substrate, with low efficiency [2].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Engemann, C., Elssner, T. and Kleber, H.P. Biotransformation of crotonobetaine to L-(–)-carnitine in Proteus sp. Arch. Microbiol. 175 (2001) 353–359. [PMID: 11409545]
2.  Elssner, T., Engemann, C., Baumgart, K. and Kleber, H.P. Involvement of coenzyme A esters and two new enzymes, an enoyl-CoA hydratase and a CoA-transferase, in the hydration of crotonobetaine to L-carnitine by Escherichia coli. Biochemistry 40 (2001) 11140–11148. [DOI] [PMID: 11551212]
3.  Engemann, C., Elssner, T., Pfeifer, S., Krumbholz, C., Maier, T. and Kleber, H.P. Identification and functional characterisation of genes and corresponding enzymes involved in carnitine metabolism of Proteus sp. Arch. Microbiol. 183 (2005) 176–189. [DOI] [PMID: 15731894]
[EC 4.2.1.149 created 2014]
 
 
EC 6.2.1.48     
Accepted name: carnitine—CoA ligase
Reaction: ATP + L-carnitine + CoA = AMP + diphosphate + L-carnitinyl-CoA
Glossary: carnitine = 3-hydroxy-4-(trimethylammonio)butanoate
crotonobetaine = (E)-4-(trimethylammonio)but-2-enoate
γ-butyrobetaine = 4-(trimethylammonio)butanoate
Other name(s): caiC (gene name)
Systematic name: L-carnitine:CoA ligase (AMP-forming)
Comments: The enzyme, originally characterized from the bacterium Escherichia coli, can catalyse the transfer of CoA to L-carnitine, crotonobetaine and γ-butyrobetaine. In vitro the enzyme also exhibits the activity of EC 2.8.3.21, L-carnitine CoA-transferase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Eichler, K., Bourgis, F., Buchet, A., Kleber, H.P. and Mandrand-Berthelot, M.A. Molecular characterization of the cai operon necessary for carnitine metabolism in Escherichia coli. Mol. Microbiol. 13 (1994) 775–786. [DOI] [PMID: 7815937]
2.  Bernal, V., Arense, P., Blatz, V., Mandrand-Berthelot, M.A., Canovas, M. and Iborra, J.L. Role of betaine:CoA ligase (CaiC) in the activation of betaines and the transfer of coenzyme A in Escherichia coli. J. Appl. Microbiol. 105 (2008) 42–50. [DOI] [PMID: 18266698]
[EC 6.2.1.48 created 2017]
 
 


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