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Literature summary for 1.14.14.154 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

Cloned(Commentary)

Cloned (Comment) Organism
gene RV0764c, coexpression with ferredoxin in Escherichia coli strain HMS174 (DE3) Mycobacterium tuberculosis

General Stability

General Stability Organism
the P450 form is stabilized by estriol Mycobacterium tuberculosis

Inhibitors

Inhibitors Comment Organism Structure
1-phenylimidazole heme iron-coordinating inhibitor Mycobacterium tuberculosis
4-phenylimidazole heme iron-coordinating inhibitor Mycobacterium tuberculosis
clotrimazole
-
Mycobacterium tuberculosis
econazole
-
Mycobacterium tuberculosis
fluconazole
-
Mycobacterium tuberculosis
ketoconazole
-
Mycobacterium tuberculosis
miconazole
-
Mycobacterium tuberculosis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information steady-state kinetic and thermodynamic analysis Mycobacterium tuberculosis

Metals/Ions

Metals/Ions Comment Organism Structure
Iron cysteinate- and aqua-ligated heme iron, P450 formation involves residue Cys394, Cys 394 thiol is deprotonated to thiolate in the ferric form, and ferredoxin-bound [3Fe-4S] iron-sulfur cluster Mycobacterium tuberculosis

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis
-
gene RV0764c
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme from Escherichia coli strain HMS174 (DE3) by two different steps of anion exchange chromatography and hydroxyapaptite chromatography to homogeneity Mycobacterium tuberculosis

Reaction

Reaction Comment Organism Reaction ID
a 14alpha-methylsteroid + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 = a DELTA14-steroid + formate + 3 [oxidized NADPH-hemoprotein reductase] + 4 H2O heme iron reduction as a rate-limiting step Mycobacterium tuberculosis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-phenylimidazole + [reduced NADPH-hemoprotein reductase] + O2 2-phenylimidazole binding causes thermally induced alterations in CYP51 active site structure and/or binding modes for the small ligand Mycobacterium tuberculosis ?
-
?
estriol + [reduced NADPH-hemoprotein reductase] + O2
-
Mycobacterium tuberculosis ?
-
?
additional information P420 formation process with protonation of Cys394 and structure by binding of CO to P450, overview Mycobacterium tuberculosis ?
-
?

Subunits

Subunits Comment Organism
More detailed spectroscopic structure analysis of enzyme with bound ligands, overview Mycobacterium tuberculosis

Synonyms

Synonyms Comment Organism
CYP51
-
Mycobacterium tuberculosis
More the enzyme belongs to the sterol demethylase family Mycobacterium tuberculosis
sterol demethylase P450
-
Mycobacterium tuberculosis

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
-
thermal inactivation kinetics Mycobacterium tuberculosis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
assay at Mycobacterium tuberculosis

Cofactor

Cofactor Comment Organism Structure
Ferredoxin Fdx binds a [3Fe-4S] iron-sulfur cluster, encoded by gene RV0763c adejacent to the gene encoding the enzyme Mycobacterium tuberculosis