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 |
References: |
1. |
Rebouche, C.J. and Engel, A.G. Tissue distribution of carnitine biosynthetic enzymes in man. Biochim. Biophys. Acta 630 (1980) 22–29. [PMID: 6770910] |
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[EC 1.2.1.47 created 1983] |
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EC |
1.14.11.1 |
Accepted name: |
γ-butyrobetaine dioxygenase |
Reaction: |
4-trimethylammoniobutanoate + 2-oxoglutarate + O2 = 3-hydroxy-4-trimethylammoniobutanoate + succinate + CO2 |
Other name(s): |
α-butyrobetaine hydroxylase; γ-butyrobetaine hydroxylase; butyrobetaine hydroxylase |
Systematic name: |
4-trimethylammoniobutanoate,2-oxoglutarate:oxygen oxidoreductase (3-hydroxylating) |
Comments: |
Requires Fe2+ and ascorbate. |
References: |
1. |
Lindstedt, G. and Lindstedt, S. Cofactor requirements of γ-butyrobetaine hydroxylase from rat liver. J. Biol. Chem. 245 (1970) 4178–4186. [PMID: 4396068] |
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[EC 1.14.11.1 created 1972] |
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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. |
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. [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. [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. [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. [PMID: 15823031] |
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[EC 2.8.3.21 created 2014] |
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