EC |
1.1.1.108 |
Accepted name: |
carnitine 3-dehydrogenase |
Reaction: |
carnitine + NAD+ = 3-dehydrocarnitine + NADH + H+ |
Systematic name: |
carnitine:NAD+ 3-oxidoreductase |
Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, MetaCyc, CAS registry number: 9045-45-8 |
References: |
1. |
Aurich, H., Kleber, H.-P., Sorger, H. and Tauchert, H. Reinigung und Eigenschaften der Carnitindehydrogenase aus Pseudomonas aeruginosa. Eur. J. Biochem. 6 (1968) 196–201. [DOI] [PMID: 4302217] |
2. |
Schöpp, W., Sorger, H., Kleber, H.-P. and Aurich, H. Kinetische Untersuchungen zum Reaktionmechanisms der Carnitindehydrogenase aus Pseudomonas aeruginosa. Eur. J. Biochem. 10 (1969) 56–60. [DOI] [PMID: 4310279] |
|
[EC 1.1.1.108 created 1972] |
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|
EC |
1.1.1.254 |
Accepted name: |
(S)-carnitine 3-dehydrogenase |
Reaction: |
(S)-carnitine + NAD+ = 3-dehydrocarnitine + NADH + H+ |
Systematic name: |
(S)-carnitine:NAD+ oxidoreductase |
Comments: |
Specific for the (S)-enantiomer of carnitine, i.e., the enantiomer of the substrate of EC 1.1.1.108 carnitine 3-dehydrogenase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 154215-16-4, 169277-49-0 |
References: |
1. |
Setyahadi, S., Ueyama, T., Arimoto, T., Mori, N. and Kitamoto, Y. Purification and properties of a new enzyme, D-carnitine dehydrogenase, from Agrobacterium sp. 525a. Biosci. Biotechnol. Biochem. 61 (1997) 1055–1058. [DOI] [PMID: 9214773] |
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[EC 1.1.1.254 created 1999] |
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EC |
1.2.1.47 |
Accepted name: |
4-trimethylammoniobutyraldehyde dehydrogenase |
Reaction: |
4-trimethylammoniobutanal + NAD+ + H2O = 4-trimethylammoniobutanoate + NADH + 2 H+ |
Other name(s): |
4-trimethylaminobutyraldehyde dehydrogenase; 4-N-trimethylaminobutyraldehyde dehydrogenase |
Systematic name: |
4-trimethylammoniobutanal:NAD+ 1-oxidoreductase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 73361-01-0 |
References: |
1. |
Rebouche, C.J. and Engel, A.G. Tissue distribution of carnitine biosynthetic enzymes in man. Biochim. Biophys. Acta 630 (1980) 22–29. [DOI] [PMID: 6770910] |
|
[EC 1.2.1.47 created 1983] |
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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] |
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[EC 1.3.8.13 created 2017] |
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EC |
1.14.11.8 |
Accepted name: |
trimethyllysine dioxygenase |
Reaction: |
N6,N6,N6-trimethyl-L-lysine + 2-oxoglutarate + O2 = (3S)-3-hydroxy-N6,N6,N6-trimethyl-L-lysine + succinate + CO2 |
Other name(s): |
trimethyllysine α-ketoglutarate dioxygenase; TML-α-ketoglutarate dioxygenase; TML hydroxylase; 6-N,6-N,6-N-trimethyl-L-lysine,2-oxoglutarate:oxygen oxidoreductase (3-hydroxylating) |
Systematic name: |
N6,N6,N6-trimethyl-L-lysine,2-oxoglutarate:oxygen oxidoreductase (3-hydroxylating) |
Comments: |
Requires Fe2+ and ascorbate. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 74622-49-4 |
References: |
1. |
Hulse, J.D., Ellis, S.R. and Henderson, L.M. Carnitine biosynthesis. β-Hydroxylation of trimethyllysine by an α-ketoglutarate-dependent mitochondrial dioxygenase. J. Biol. Chem. 253 (1978) 1654–1659. [PMID: 627563] |
2. |
Al Temimi, A.H., Pieters, B.J., Reddy, Y.V., White, P.B. and Mecinovic, J. Substrate scope for trimethyllysine hydroxylase catalysis. Chem. Commun. (Camb.) 52 (2016) 12849–12852. [PMID: 27730239] |
3. |
Lesniak, R.K., Markolovic, S., Tars, K. and Schofield, C.J. Human carnitine biosynthesis proceeds via (2S,3S)-3-hydroxy-Nε-trimethyllysine. Chem. Commun. (Camb.) 53 (2016) 440–442. [PMID: 27965989] |
4. |
Reddy, Y.V., Al Temimi, A.H., White, P.B. and Mecinovic, J. Evidence that trimethyllysine hydroxylase catalyzes the formation of (2S,3S)-3-hydroxy-Nε-trimethyllysine. Org. Lett. 19 (2017) 400–403. [PMID: 28045275] |
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[EC 1.14.11.8 created 1983] |
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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, PDB |
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] |
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[EC 1.14.13.239 created 2017] |
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EC |
2.1.1.383 |
Accepted name: |
L-carnitine—corrinoid protein Co-methyltransferase |
Reaction: |
L-carnitine + a [Co(I) quaternary-amine-specific corrinoid protein] = a [methyl-Co(III) quaternary-amine-specific corrinoid protein] + L-norcarnitine |
Glossary: |
L-norcarnitine = (3R)-4-(dimethylamino)-3-hydroxybutanoate |
Other name(s): |
mtcB (gene name) |
Systematic name: |
L-carnitine:[Co(I) quaternary-amine-specific corrinoid protein] Co-methyltransferase |
Comments: |
The enzyme, characterized from the bacterium Eubacterium limosum, is a component of a system that transfers a methyl group from L-carnitine to tetrahydrofolate, as part of an L-carnitine degradation pathway. The resulting 5-methyltetrahydrofolate is processed to acetyl-CoA via the Wood—Ljungdahl pathway. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Kountz, D.J., Behrman, E.J., Zhang, L. and Krzycki, J.A. MtcB, a member of the MttB superfamily from the human gut acetogen Eubacterium limosum, is a cobalamin-dependent carnitine demethylase. J. Biol. Chem. 295 (2020) 11971–11981. [DOI] [PMID: 32571881] |
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[EC 2.1.1.383 created 2021] |
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EC |
2.1.1.389 |
Accepted name: |
[methyl-Co(III) quaternary-amine-specific corrinoid protein]—tetrahydrofolate methyltransferase |
Reaction: |
a [methyl-Co(III) quaternary-amine-specific corrinoid protein] + tetrahydrofolate = N5-methyltetrahydrofolate + a [Co(I) quaternary-amine-specific corrinoid protein] |
Other name(s): |
mtqA (gene name) (ambiguous); [methyl-Co(III) MtqC corrinoid protein]—tetrahydrofolate methyltransferase |
Systematic name: |
[methyl-Co(III) quaternary-amine-specific corrinoid protein]:tetrahydrofolate methyltransferase |
Comments: |
The enzyme, characterized from the acetogenic gut bacterium Eubacterium limosum, participates in a pathway for the degradation of some quaternary amine compounds (L-proline betaine and L-carnitine). The enzyme catalyses the transfer of a methyl group bound to the cobalt cofactor of a dedicated corrinoid protein (bacterial MtqC) to tetrahydrofolate. The resulting 5-methyltetrahydrofolate is processed to acetyl-CoA via the Wood—Ljungdahl pathway. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Picking, J.W., Behrman, E.J., Zhang, L. and Krzycki, J.A. MtpB, a member of the MttB superfamily from the human intestinal acetogen Eubacterium limosum, catalyzes proline betaine demethylation. J. Biol. Chem. 294 (2019) 13697–13707. [DOI] [PMID: 31341018] |
2. |
Kountz, D.J., Behrman, E.J., Zhang, L. and Krzycki, J.A. MtcB, a member of the MttB superfamily from the human gut acetogen Eubacterium limosum, is a cobalamin-dependent carnitine demethylase. J. Biol. Chem. 295 (2020) 11971–11981. [DOI] [PMID: 32571881] |
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[EC 2.1.1.389 created 2023] |
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EC |
2.3.1.6 |
Accepted name: |
choline O-acetyltransferase |
Reaction: |
acetyl-CoA + choline = CoA + O-acetylcholine |
Other name(s): |
choline acetylase; choline acetyltransferase |
Systematic name: |
acetyl-CoA:choline O-acetyltransferase |
Comments: |
Propanoyl-CoA can act, more slowly, in place of acetyl-CoA. |
Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9012-78-6 |
References: |
1. |
Berman, R., Wilson, I.B. and Nachmansohn, D. Choline acetylase specificity in relation to biological function. Biochim. Biophys. Acta 12 (1953) 315–324. [DOI] [PMID: 13115440] |
2. |
Berry, J.F. and Whittaker, V.P. The acyl-group specificity of choline acetylase. Biochem. J. 73 (1959) 447–458. [PMID: 13799882] |
3. |
Fritz, I.B. and Schultz, S.K. Carnitine acetyltransferase. II. Inhibition by carnitine analogues and by sulfhydryl reagents. J. Biol. Chem. 240 (1965) 2188–2192. [PMID: 14299645] |
4. |
Schuberth, J. Choline acetyltransferase. Purification and effect of salts on the mechanism of the enzyme-catalysed reaction. Biochim. Biophys. Acta 122 (1966) 470–481. |
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[EC 2.3.1.6 created 1961] |
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EC |
2.3.1.7 |
Accepted name: |
carnitine O-acetyltransferase |
Reaction: |
acetyl-CoA + carnitine = CoA + O-acetylcarnitine |
Other name(s): |
acetyl-CoA-carnitine O-acetyltransferase; acetylcarnitine transferase; carnitine acetyl coenzyme A transferase; carnitine acetylase; carnitine acetyltransferase; carnitine-acetyl-CoA transferase; CATC |
Systematic name: |
acetyl-CoA:carnitine O-acetyltransferase |
Comments: |
Also acts on propanoyl-CoA and butanoyl-CoA (cf. EC 2.3.1.21 carnitine O-palmitoyltransferase and EC 2.3.1.137 carnitine O-octanoyltransferase). |
Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9029-90-7 |
References: |
1. |
Chase, J.F.A., Pearson, D.J. and Tubbs, P.K. The preparation of crystalline carnitine acetyltransferase. Biochim. Biophys. Acta 96 (1965) 162–165. [DOI] [PMID: 14285260] |
2. |
Friedman, S. and Fraenkel, G. Reversible enzymatic acetylation of carnitine. Arch. Biochem. Biophys. 59 (1955) 491–501. [DOI] [PMID: 13275966] |
3. |
Miyazawa, S., Ozasa, H., Furuta, S., Osumi, T. and Hashimoto, T. Purification and properties of carnitine acetyl transferase from rat liver. J. Biochem. (Tokyo) 93 (1983) 439–451. [PMID: 6404901] |
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[EC 2.3.1.7 created 1961] |
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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] |
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[EC 2.3.1.21 created 1972] |
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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] |
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[EC 2.3.1.137 created 1992] |
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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, PDB |
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] |
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[EC 2.8.3.21 created 2014] |
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EC |
3.1.1.1 |
Accepted name: |
carboxylesterase |
Reaction: |
a carboxylic ester + H2O = an alcohol + a carboxylate |
|
For diagram of retinal and derivatives biosynthesis, click here |
Other name(s): |
ali-esterase; B-esterase; monobutyrase; cocaine esterase; procaine esterase; methylbutyrase; vitamin A esterase; butyryl esterase; carboxyesterase; carboxylate esterase; carboxylic esterase; methylbutyrate esterase; triacetin esterase; carboxyl ester hydrolase; butyrate esterase; methylbutyrase; α-carboxylesterase; propionyl esterase; nonspecific carboxylesterase; esterase D; esterase B; esterase A; serine esterase; carboxylic acid esterase; cocaine esterase |
Systematic name: |
carboxylic-ester hydrolase |
Comments: |
Wide specificity. The enzymes from microsomes also catalyse the reactions of EC 3.1.1.2 (arylesterase), EC 3.1.1.5 (lysophospholipase), EC 3.1.1.6 (acetylesterase), EC 3.1.1.23 (acylglycerol lipase), EC 3.1.1.28 (acylcarnitine hydrolase), EC 3.1.2.2 (palmitoyl-CoA hydrolase), EC 3.5.1.4 (amidase) and EC 3.5.1.13 (aryl-acylamidase). Also hydrolyses vitamin A esters. |
Links to other databases: |
BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9016-18-6 |
References: |
1. |
Augusteyn, R.C., de Jersey, J., Webb, E.C. and Zerner, B. On the homology of the active-site peptides of liver carboxylesterases. Biochim. Biophys. Acta 171 (1969) 128–137. [DOI] [PMID: 4884138] |
2. |
Barker, D.L. and Jencks, W.P. Pig liver esterase. Physical properties. Biochemistry 8 (1969) 3879–3889. [PMID: 4981346] |
3. |
Bertram, J. and Krisch, K. Hydrolysis of vitamin A acetate by unspecific carboxylesterases from liver and kidney. Eur. J. Biochem. 11 (1969) 122–126. [DOI] [PMID: 5353595] |
4. |
Burch, J. The purification and properties of horse liver esterase. Biochem. J. 58 (1954) 415–426. [PMID: 13208632] |
5. |
Horgan, D.J., Stoops, J.K., Webb, E.C. and Zerner, B. Carboxylesterases (EC 3.1.1). A large-scale purification of pig liver carboxylesterase. Biochemistry 8 (1969) 2000–2006. [PMID: 5785220] |
6. |
Malhotra, O.P. and Philip, G. Specificity of goat intestinal esterase. Biochem. Z. 346 (1966) 386–402. |
7. |
Mentlein, R., Schumann, M. and Heymann, E. Comparative chemical and immunological characterization of five lipolytic enzymes (carboxylesterases) from rat liver microsomes. Arch. Biochem. Biophys. 234 (1984) 612–621. [DOI] [PMID: 6208846] |
8. |
Runnegar, M.T.C., Scott, K., Webb, E.C. and Zerner, B. Carboxylesterases (EC 3.1.1). Purification and titration of ox liver carboxylesterase. Biochemistry 8 (1969) 2013–2018. [PMID: 5785222] |
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[EC 3.1.1.1 created 1961] |
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|
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, PDB, 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] |
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[EC 3.1.1.28 created 1972] |
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EC |
3.1.2.33 |
Accepted name: |
betainyl-CoA thioesterase |
Reaction: |
betaine-CoA + H2O = glycine betaine + CoA |
Glossary: |
betaine-CoA = glycinebetainyl-CoA = betainyl-CoA = N,N,N-trimethylglycyl-CoA |
Other name(s): |
cdhB (gene name) |
Systematic name: |
betaine-CoA hydrolase |
Comments: |
The enzyme, characterized from the bacterium Pseudomonas aeruginosa, is involved in an L-carnitine degradation pathway. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Wargo, M.J. and Hogan, D.A. Identification of genes required for Pseudomonas aeruginosa carnitine catabolism. Microbiology (Reading) 155 (2009) 2411–2419. [DOI] [PMID: 19406895] |
2. |
Bastard, K., Smith, A.A., Vergne-Vaxelaire, C., Perret, A., Zaparucha, A., De Melo-Minardi, R., Mariage, A., Boutard, M., Debard, A., Lechaplais, C., Pelle, C., Pellouin, V., Perchat, N., Petit, J.L., Kreimeyer, A., Medigue, C., Weissenbach, J., Artiguenave, F., De Berardinis, V., Vallenet, D. and Salanoubat, M. Revealing the hidden functional diversity of an enzyme family. Nat. Chem. Biol. 10 (2014) 42–49. [DOI] [PMID: 24240508] |
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[EC 3.1.2.33 created 2024] |
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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. |
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[EC 3.5.1.73 created 1992] |
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EC |
4.1.1.42 |
Accepted name: |
carnitine decarboxylase |
Reaction: |
carnitine = 2-methylcholine + CO2 |
Other name(s): |
carnitine carboxy-lyase |
Systematic name: |
carnitine carboxy-lyase (2-methylcholine-forming) |
Comments: |
Requires ATP. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37237-38-0 |
References: |
1. |
Khairallah, E.A. and Wolf, G. Carnitine decarboxylase. The conversion of carnitine to β-methylcholine. J. Biol. Chem. 242 (1967) 32–39. [PMID: 6016331] |
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[EC 4.1.1.42 created 1972] |
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EC
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4.2.1.89
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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] |
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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] |
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[EC 4.2.1.149 created 2014] |
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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] |
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[EC 6.2.1.48 created 2017] |
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