Adenosylcobyric acid synthase (glutamine-hydrolysing)
| Adenosylcobyric acid synthase (glutamine-hydrolyzing) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 6.3.5.10 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, an adenosylcobyric acid synthase (glutamine-hydrolysing) (EC 6.3.5.10) is an enzyme that catalyzes the chemical reaction
- 4 ATP + adenosylcobyrinic acid a,c-diamide + 4 L-glutamine + 4 H2O 4 ADP + 4 phosphate + adenosylcobyric acid + 4 L-glutamate
The four substrates of this enzyme are ATP, adenosylcobyrinic acid a,c-diamide, L-glutamine, and H2O; its four products are ADP, phosphate, adenosylcobyric acid, and L-glutamate.
This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds carbon-nitrogen ligases with glutamine as amido-N-donor (Glutamine amidotransferases). The systematic name of this enzyme class is adenosylcobyrinic-acid-a,c-diamide:L-glutamine amido-ligase (ADP-forming). This enzyme is part of the biosynthetic pathway to cobalamin (vitamin B12) in bacteria.
See also
[edit]References
[edit]- Blanche F, Couder M, Debussche L, Thibaut D, Cameron B, Crouzet J (1991). "Biosynthesis of vitamin B12: stepwise amidation of carboxyl groups b, d, e, and g of cobyrinic acid a,c-diamide is catalyzed by one enzyme in Pseudomonas denitrificans". J. Bacteriol. 173 (19): 6046–51. PMC 208350. PMID 1917839.
- Warren MJ, Raux E, Schubert HL, Escalante-Semerena JC (2002). "The biosynthesis of adenosylcobalamin (vitamin B12)". Nat. Prod. Rep. 19 (4): 390–412. doi:10.1039/b108967f. PMID 12195810.
