EC Number | Cloned (Comment) | Organism |
---|---|---|
1.14.14.154 | gene RV0764c, coexpression with ferredoxin in Escherichia coli strain HMS174 (DE3) | Mycobacterium tuberculosis |
EC Number | General Stability | Organism |
---|---|---|
1.14.14.154 | the P450 form is stabilized by estriol | Mycobacterium tuberculosis |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
1.14.14.154 | 1-phenylimidazole | heme iron-coordinating inhibitor | Mycobacterium tuberculosis | |
1.14.14.154 | 4-phenylimidazole | heme iron-coordinating inhibitor | Mycobacterium tuberculosis | |
1.14.14.154 | clotrimazole | - |
Mycobacterium tuberculosis | |
1.14.14.154 | econazole | - |
Mycobacterium tuberculosis | |
1.14.14.154 | fluconazole | - |
Mycobacterium tuberculosis | |
1.14.14.154 | ketoconazole | - |
Mycobacterium tuberculosis | |
1.14.14.154 | miconazole | - |
Mycobacterium tuberculosis |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.14.14.154 | additional information | - |
additional information | steady-state kinetic and thermodynamic analysis | Mycobacterium tuberculosis |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
1.14.14.154 | 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 |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.14.14.154 | Mycobacterium tuberculosis | - |
gene RV0764c | - |
EC Number | Purification (Comment) | Organism |
---|---|---|
1.14.14.154 | recombinant enzyme from Escherichia coli strain HMS174 (DE3) by two different steps of anion exchange chromatography and hydroxyapaptite chromatography to homogeneity | Mycobacterium tuberculosis |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
1.14.14.154 | 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 |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.14.14.154 | 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 | ? | - |
? | |
1.14.14.154 | estriol + [reduced NADPH-hemoprotein reductase] + O2 | - |
Mycobacterium tuberculosis | ? | - |
? | |
1.14.14.154 | additional information | P420 formation process with protonation of Cys394 and structure by binding of CO to P450, overview | Mycobacterium tuberculosis | ? | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
1.14.14.154 | More | detailed spectroscopic structure analysis of enzyme with bound ligands, overview | Mycobacterium tuberculosis |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.14.14.154 | CYP51 | - |
Mycobacterium tuberculosis |
1.14.14.154 | More | the enzyme belongs to the sterol demethylase family | Mycobacterium tuberculosis |
1.14.14.154 | sterol demethylase P450 | - |
Mycobacterium tuberculosis |
EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|---|
1.14.14.154 | additional information | - |
thermal inactivation kinetics | Mycobacterium tuberculosis |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
1.14.14.154 | 7.5 | - |
assay at | Mycobacterium tuberculosis |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.14.14.154 | Ferredoxin | Fdx binds a [3Fe-4S] iron-sulfur cluster, encoded by gene RV0763c adejacent to the gene encoding the enzyme | Mycobacterium tuberculosis |