EC |
1.14.15.27 |
Accepted name: |
β-dihydromenaquinone-9 ω-hydroxylase |
Reaction: |
β-dihydromenaquinone-9 + 2 reduced ferredoxin [iron-sulfur] cluster + O2 = ω-hydroxy-β-dihydromenaquinone-9 + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O |
|
For diagram of vitamin K biosynthesis, click here |
Glossary: |
β-dihydromenaquinone-9 = MK-9(II-H2) = 2-methyl-3-[(2E,10E,14E,18E,22E,26E,30E,33E)-3,7,11,15,19,23,27,31,35-nonamethylhexatriaconta-2,10,14,18,22,26,30,33-octaen-1-yl]naphthalene-1,4-dione |
Other name(s): |
cyp128 (gene name) |
Systematic name: |
β-dihydromenaquinone-9,reduced ferredoxin:oxygen oxidoreductase (ω-hydroxylating) |
Comments: |
The bacterial cytochrome P-450 enzyme is involved in the biosynthesis of ω-sulfo-β-dihydromenaquinone-9 by members of the Mycobacterium tuberculosis complex. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Holsclaw, C.M., Sogi, K.M., Gilmore, S.A., Schelle, M.W., Leavell, M.D., Bertozzi, C.R. and Leary, J.A. Structural characterization of a novel sulfated menaquinone produced by stf3 from Mycobacterium tuberculosis. ACS Chem. Biol. 3 (2008) 619–624. [PMID: 18928249] |
2. |
Sogi, K.M., Holsclaw, C.M., Fragiadakis, G.K., Nomura, D.K., Leary, J.A. and Bertozzi, C.R. Biosynthesis and regulation of sulfomenaquinone, a metabolite associated with virulence in Mycobacterium tuberculosis. ACS Infect Dis 2 (2016) 800–806. [PMID: 27933784] |
|
[EC 1.14.15.27 created 2018] |
|
|
|
|