1.14.15.27: beta-dihydromenaquinone-9 omega-hydroxylase
This is an abbreviated version!
For detailed information about beta-dihydromenaquinone-9 omega-hydroxylase, go to the full flat file.
Reaction
+ 2 reduced ferredoxin [iron-sulfur] cluster + = + 2 oxidized ferredoxin [iron-sulfur] cluster +
Synonyms
cyp128, Rv2268c
ECTree
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General Information
General Information on EC 1.14.15.27 - beta-dihydromenaquinone-9 omega-hydroxylase
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physiological function
Cyp128 and sulfotransferase Stf 3 are sufficient for the biosynthesis of sulfomenaquinone from menaquinone in recombinant Mycobacterium smegmatis. In a mouse model of infection the loss of Cyp128 exhibits a hypervirulent phenotype similar to that in previous studies of the Stf 3 mutant
physiological function
Cyp128 is the enzyme responsible for the terminal oxidation of the polyisoprenoid chain of dihydromenaquinone-9, thereby allowing sulfation of the resulting hydroxyl moiety by Stf3. The sulfated metabolite S881 is associated with virulence in Mycobacterium tuberculosis
physiological function
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Cyp128 is the enzyme responsible for the terminal oxidation of the polyisoprenoid chain of dihydromenaquinone-9, thereby allowing sulfation of the resulting hydroxyl moiety by Stf3. The sulfated metabolite S881 is associated with virulence in Mycobacterium tuberculosis
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physiological function
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Cyp128 and sulfotransferase Stf 3 are sufficient for the biosynthesis of sulfomenaquinone from menaquinone in recombinant Mycobacterium smegmatis. In a mouse model of infection the loss of Cyp128 exhibits a hypervirulent phenotype similar to that in previous studies of the Stf 3 mutant
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