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Literature summary extracted from

  • Bellamine, A.; Mangla, A.T.; Nes, W.D.; Waterman, M.R.
    Characterization and catalytic properties of the sterol 14alpha-demethylase from Mycobacterium tuberculosis (1999), Proc. Natl. Acad. Sci. USA, 96, 8937-8942 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.14.15.36 expression in Escherichia coli Mycobacterium tuberculosis

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.14.15.36 cytosol
-
Mycobacterium tuberculosis 5829
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Organism

EC Number Organism UniProt Comment Textmining
1.14.15.36 Mycobacterium tuberculosis P9WPP9
-
-
1.14.15.36 Mycobacterium tuberculosis H37Rv P9WPP9
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-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.15.36 24,25-dihydrolanosterol + 6 reduced ferredoxin [iron-sulfur] cluster + 6 H+ + 3 O2
-
Mycobacterium tuberculosis 4,4-dimethyl-5alpha-cholesta-8,14-diene-3beta-ol + formate + 6 oxidized ferredoxin [iron-sulfur] cluster + 4 H2O
-
?
1.14.15.36 24,25-dihydrolanosterol + 6 reduced ferredoxin [iron-sulfur] cluster + 6 H+ + 3 O2
-
Mycobacterium tuberculosis H37Rv 4,4-dimethyl-5alpha-cholesta-8,14-diene-3beta-ol + formate + 6 oxidized ferredoxin [iron-sulfur] cluster + 4 H2O
-
?
1.14.15.36 lanosterol + 6 reduced ferredoxin [iron-sulfur] cluster + 6 H+ + 3 O2
-
Mycobacterium tuberculosis 4,4-dimethylzymosterol + formate + 6 oxidized ferredoxin [iron-sulfur] cluster + 4 H2O
-
?
1.14.15.36 lanosterol + 6 reduced ferredoxin [iron-sulfur] cluster + 6 H+ + 3 O2
-
Mycobacterium tuberculosis H37Rv 4,4-dimethylzymosterol + formate + 6 oxidized ferredoxin [iron-sulfur] cluster + 4 H2O
-
?
1.14.15.36 additional information both flavodoxin and ferredoxin redox systems are able to support the enzymatic activity. Substrates require a 14alpha methyl group and a 8,9 C-C double bond Mycobacterium tuberculosis ?
-
?
1.14.15.36 additional information both flavodoxin and ferredoxin redox systems are able to support the enzymatic activity. Substrates require a 14alpha methyl group and a 8,9 C-C double bond Mycobacterium tuberculosis H37Rv ?
-
?
1.14.15.36 obtusifoliol + 6 reduced ferredoxin [iron-sulfur] cluster + 6 H+ + 3 O2
-
Mycobacterium tuberculosis 4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + 6 oxidized ferredoxin [iron-sulfur] cluster + 4 H2O
-
?
1.14.15.36 obtusifoliol + 6 reduced ferredoxin [iron-sulfur] cluster + 6 H+ + 3 O2
-
Mycobacterium tuberculosis H37Rv 4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + 6 oxidized ferredoxin [iron-sulfur] cluster + 4 H2O
-
?

Subunits

EC Number Subunits Comment Organism
1.14.15.36 ? x * 50000, SDS-PAGE, x * 51400, calculated from sequence Mycobacterium tuberculosis

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.15.36 cytochrome P450 the oxidized absolute spectrum of the purified enzyme, in the absence of substrate, shows a Soret band at 417 nm and alpha-,beta-, and delta bands at 569, 535, and 369 nm Mycobacterium tuberculosis