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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]

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.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9045-31-2

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]

[EC 1.14.11.1 created 1972]

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]

[EC 2.8.3.21 created 2014]