Precorrin-3B synthase
| Precorrin-3B synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.14.13.83 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
Precorrin-3B synthase (EC 1.14.13.83) is an enzyme that catalyzes the chemical reaction
The four substrates of this enzyme are precorrin-3A, reduced nicotinamide adenine dinucleotide (NADH), oxygen, and a proton. Its products are precorrin-3B, oxidised NAD+, and water.[1][2][3]
This enzyme is an iron–sulfur protein acting as an oxidoreductase, with molecular oxygen as oxidant and incorporating one of its atoms. The systematic name of this enzyme class is precorrin-3A,NADH:oxygen oxidoreductase (20-hydroxylating). Other names in common use include precorrin-3X synthase, and CobG. This enzyme is part of the biosynthetic pathway to cobalamin (vitamin B12) in aerobic bacteria.[4]
See also
[edit]References
[edit]- ↑ Debussche L, Thibaut D, Cameron B, Crouzet J, Blanche F (1993). "Biosynthesis of the corrin macrocycle of coenzyme B12 in Pseudomonas denitrificans". J. Bacteriol. 175 (22): 7430–40. doi:10.1128/jb.175.22.7430-7440.1993. PMC 206888. PMID 8226690.
- ↑ Scott AI, Roessner CA, Stolowich NJ, Spencer JB, Min C, Ozaki SI (1993). "Biosynthesis of vitamin B12. Discovery of the enzymes for oxidative ring contraction and insertion of the fourth methyl group". FEBS Lett. 331 (1–2): 105–8. Bibcode:1993FEBSL.331..105S. doi:10.1016/0014-5793(93)80306-F. PMID 8405386.
- ↑ 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.
- ↑ Enzyme 1.14.13.83 at KEGG Pathway Database.
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