5,6-dimethylbenzimidazole synthase
| 5,6-dimethylbenzimidazole synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.14.99.40 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
5,6-dimethylbenzimidazole synthase (EC 1.14.99.40, BluB) is an enzyme with systematic name FMNH2 oxidoreductase (5,6-dimethylbenzimidazole forming).[1][2][3] This enzyme catalyses the following chemical reaction
- FMNH2 + NADH + H+ + O2 5,6-dimethylbenzimidazole + D-erythrose 4-phosphate + NAD+ + other product
The C-2 of 5,6-dimethylbenzimidazole is derived from C-1' of the ribityl group of FMNH2 and 2-H from the ribityl 1'-pro-S hydrogen. This enzyme is part of the biosynthetic pathway to cobalamin (vitamin B12) in bacteria.
See also
[edit]References
[edit]- ^ Gray MJ, Escalante-Semerena JC (February 2007). "Single-enzyme conversion of FMNH2 to 5,6-dimethylbenzimidazole, the lower ligand of B12". Proceedings of the National Academy of Sciences of the United States of America. 104 (8): 2921–6. Bibcode:2007PNAS..104.2921G. doi:10.1073/pnas.0609270104. PMC 1815282. PMID 17301238.
- ^ Ealick SE, Begley TP (March 2007). "Biochemistry: molecular cannibalism". Nature. 446 (7134): 387–8. Bibcode:2007Natur.446..387E. doi:10.1038/446387a. PMID 17377573.
- ^ Taga ME, Larsen NA, Howard-Jones AR, Walsh CT, Walker GC (March 2007). "BluB cannibalizes flavin to form the lower ligand of vitamin B12". Nature. 446 (7134): 449–53. Bibcode:2007Natur.446..449T. doi:10.1038/nature05611. PMC 2770582. PMID 17377583.
External links
[edit]- 5,6-dimethylbenzimidazole+synthase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
