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Literature summary extracted from

  • Holsclaw, C.; Sogi, K.; Gilmore, S.; Schelle, M.; Leavell, M.; Bertozzi, C.; Leary, J.
    Structural characterization of a novel sulfated menaquinone produced by stf3 from Mycobacterium tuberculosis (2008), ACS Chem. Biol., 3, 619-624 .
    View publication on PubMedView publication on EuropePMC

Organism

EC Number Organism UniProt Comment Textmining
1.14.15.27 Mycobacterium tuberculosis P9WPN7
-
-
1.14.15.27 Mycobacterium tuberculosis H37Rv P9WPN7
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-
2.8.2.40 Mycobacterium tuberculosis
-
-
-
2.8.2.40 Mycobacterium tuberculosis H37Rv
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.8.2.40 3'-phosphoadenylyl sulfate + dihydromenaquinone-9
-
Mycobacterium tuberculosis adenosine 3',5'-bisphosphate + S881
-
?
2.8.2.40 3'-phosphoadenylyl sulfate + dihydromenaquinone-9
-
Mycobacterium tuberculosis H37Rv adenosine 3',5'-bisphosphate + S881
-
?

Synonyms

EC Number Synonyms Comment Organism
1.14.15.27 cyp128
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Mycobacterium tuberculosis
2.8.2.40 stf3
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Mycobacterium tuberculosis

General Information

EC Number General Information Comment Organism
1.14.15.27 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 Mycobacterium tuberculosis