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Your query returned 1 entry. 
Printable version
| EC | 2.6.1.121 | ||
| Accepted name: | 8-amino-7-oxononanoate carboxylating dehydrogenase | ||
| Reaction: | (8S)-8-amino-7-oxononanoate + [protein]-L-lysine + CO2 = (7R,8S)-8-amino-7-(carboxyamino)nonanoate + [protein]-(S)-2-amino-6-oxohexanoate (overall reaction) (1a) (8S)-8-amino-7-oxononanoate + [protein]-L-lysine + NAD(P)H + H+ = [protein]-N6-[(2S,3R)-2-amino-8-carboxyoctan-3-yl]-L-lysine + H2O + NAD(P)+ (1b) [protein]-N6-[(2S,3R)-2-amino-8-carboxyoctan-3-yl]-L-lysine + CO2 + H2O + NAD(P)+ = (7R,8S)-8-amino-7-(carboxyamino)nonanoate + [protein]-(S)-2-amino-6-oxohexanoate + NAD(P)H + H+ |
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| Other name(s): | bioU (gene name) | ||
| Systematic name: | (8S)-8-amino-7-oxononanoate:[protein]-L-lysine aminotransferase (N-carboxylating) | ||
| Comments: | The enzyme, which participates in biotin biosynthesis, is found in haloarchaea and some cyanobacteria. It forms a conjugant between (7R,8S)-8-amino-7-oxononanoate and an internal lysine residue and catalyses multiple reactions, including a reduction, a carboxylation of the ε-amino group of the lysine residue, and an oxidative cleavage of the conjugate to release (7R,8S)-8-amino-7-(carboxyamino)nonanoate. During this process the lysine residue serves as an amino donor and is converted to (S)-2-amino-6-oxohexanoate, resulting in inactivation of the enzyme following a single turnover. cf. EC 2.6.1.105, lysine—8-amino-7-oxononanoate transaminase. | ||
| Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | ||
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