ENZYME entry: EC 7.2.4.5
Accepted Name |
Glutaconyl-CoA decarboxylase.
|
Alternative Name(s) |
4-carboxybut-2-enoyl-CoA carboxy-lyase. |
Glutaconyl coenzyme A decarboxylase. |
Pent-2-enoyl-CoA carboxy-lyase. |
Reaction catalysed |
4-carboxybut-2-enoyl-CoA + Na(+)(Side 1) <=> but-2-enoyl-CoA + CO(2) + Na(+)(Side 2) |
Cofactor(s) |
Biotin.
|
Comment(s) |
- The enzyme from the bacterium Acidaminococcus fermentans is a
biotinyl-protein, requires Na(+), and acts as a sodium pump.
- Prior to the Na(+)-dependent decarboxylation, the carboxylate is
transferred to biotin in a Na(+)-independent manner.
- The conserved lysine, to which biotin forms an amide bond, is located
34 amino acids before the C-terminus, flanked on both sides by two
methionine residues, which are conserved in every biotin-dependent
enzyme.
|
Cross-references |
PROSITE | PDOC00167 ; PDOC50980 |
BRENDA | 7.2.4.5 |
EC2PDB | 7.2.4.5 |
ExplorEnz | 7.2.4.5 |
PRIAM enzyme-specific profiles | 7.2.4.5 |
KEGG Ligand Database for Enzyme Nomenclature | 7.2.4.5 |
IUBMB Enzyme Nomenclature | 7.2.4.5 |
IntEnz | 7.2.4.5 |
MEDLINE | Find literature relating to 7.2.4.5 |
MetaCyc | 7.2.4.5 |
Rhea expert-curated reactions | 7.2.4.5 |
UniProtKB/Swiss-Prot |
|
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