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Literature summary for 1.14.15.36 extracted from

  • McLean, K.J.; Warman, A.J.; Seward, H.E.; Marshall, K.R.; Girvan, H.M.; Cheesman, M.R.; Waterman, M.R.; Munro, A.W.
    Biophysical characterization of the sterol demethylase P450 from Mycobacterium tuberculosis, its cognate ferredoxin, and their interactions (2006), Biochemistry, 45, 8427-8443 .
    View publication on PubMed
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Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Mycobacterium tuberculosis

Metals/Ions

Metals/Ions Comment Organism Structure
Iron
-
 Mycobacterium tuberculosis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
estriol + 6 reduced ferredoxin [iron-sulfur] cluster + 6 H+ + 3 O2 Mycobacterium tuberculosis
-
 ? + formate + 6 oxidized ferredoxin [iron-sulfur] cluster + 4 H2O
-
 ?
estriol + 6 reduced ferredoxin [iron-sulfur] cluster + 6 H+ + 3 O2 Mycobacterium tuberculosis H37Rv
-
 ? + formate + 6 oxidized ferredoxin [iron-sulfur] cluster + 4 H2O
-
 ?

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis P9WPP9
-
-
Mycobacterium tuberculosis H37Rv P9WPP9
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant protein Mycobacterium tuberculosis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
estriol + 6 reduced ferredoxin [iron-sulfur] cluster + 6 H+ + 3 O2
-
 Mycobacterium tuberculosis ? + formate + 6 oxidized ferredoxin [iron-sulfur] cluster + 4 H2O
-
 ?
estriol + 6 reduced ferredoxin [iron-sulfur] cluster + 6 H+ + 3 O2
-
 Mycobacterium tuberculosis H37Rv ? + formate + 6 oxidized ferredoxin [iron-sulfur] cluster + 4 H2O
-
 ?

Synonyms

Synonyms Comment Organism
CYP51
-
 Mycobacterium tuberculosis
sterol demethylase 450
-
 Mycobacterium tuberculosis

Cofactor

Cofactor Comment Organism Structure
Ferredoxin
-
 Mycobacterium tuberculosis
heme heme-iron reduction is the rate limiting step in catalysis. Protonation of the cysteinate ligand to the ferrous CYP51 underlies the collapse of the Fe(II)-CO adduct of the enzyme from its P450 to its P420 form. The protonation is reversible and the rate of P420 formation is substantially retarded in the estriol-bound form of CYP51 Mycobacterium tuberculosis