EC |
1.3.99.38 |
Accepted name: |
menaquinone-9 β-reductase |
Reaction: |
menaquinone-9 + reduced acceptor = β-dihydromenaquinone-9 + acceptor |
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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): |
MenJ |
Systematic name: |
menaquinone-9 oxidoreductase (β-dihydromenaquinone-9-forming) |
Comments: |
The enzyme from the bacterium Mycobacterium tuberculosis reduces the β-isoprene unit of menaquinone-9, forming the predominant form of menaquinone found in mycobacteria. Contains FAD. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Upadhyay, A., Fontes, F.L., Gonzalez-Juarrero, M., McNeil, M.R., Crans, D.C., Jackson, M. and Crick, D.C. Partial saturation of menaquinone in Mycobacterium tuberculosis: function and essentiality of a novel reductase, MenJ. ACS Cent. Sci. 1 (2015) 292–302. [DOI] [PMID: 26436137] |
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[EC 1.3.99.38 created 2017] |
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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 |
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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] |
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[EC 1.14.15.27 created 2018] |
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EC |
2.8.2.40 |
Accepted name: |
ω-hydroxy-β-dihydromenaquinone-9 sulfotransferase |
Reaction: |
3′-phosphoadenylyl sulfate + ω-hydroxy-β-dihydromenaquinone-9 = adenosine 3′,5′-bisphosphate + ω-sulfo-β-dihydromenaquinone-9 |
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): |
stf3 (gene name) |
Systematic name: |
3′-phosphoadenylyl-sulfate:ω-hydroxy-β-dihydromenaquinone-9 sulfotransferase |
Comments: |
The enzyme catalyses the last step in the production of ω-sulfo-β-dihydromenaquinone-9 by members of the Mycobacterium tuberculosis complex. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Mougous, J.D., Senaratne, R.H., Petzold, C.J., Jain, M., Lee, D.H., Schelle, M.W., Leavell, M.D., Cox, J.S., Leary, J.A., Riley, L.W. and Bertozzi, C.R. A sulfated metabolite produced by stf3 negatively regulates the virulence of Mycobacterium tuberculosis. Proc. Natl. Acad. Sci. USA 103 (2006) 4258–4263. [PMID: 16537518] |
2. |
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] |
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[EC 2.8.2.40 created 2021] |
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