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Your query returned 4 entries. Printable version
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. | ||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9045-31-2 | ||||||||||
References: |
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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: |
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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 |
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Glossary: | L-carnitine = (3R)-3-hydroxy-4-(trimethylammonio)butanoate (E)-4-(trimethylammonio)but-2-enoate = crotonobetaine 4-trimethylammoniobutanoate = γ-butyrobetaine |
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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: |
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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 |
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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 | ||||||||||
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