Cloned (Comment) | Organism |
---|---|
expressed in Escherichia coli DH5alpha cells | Mycobacterium tuberculosis |
Crystallization (Comment) | Organism |
---|---|
enzyme bound to cholest-4-en-3-one, hanging drop vapor diffusion method, using 0.2 M ammonium sulfate, 0.1 M bis-Tris, pH 5.5, and 25% (w/v) PEG 3350 | Mycobacterium tuberculosis |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
27-hydroxycholest-4-en-3-one + 4 reduced ferredoxin [iron-sulfur] cluster + 4 H+ + O2 | Mycobacterium tuberculosis | - |
cholest-4-en-3-one-27-oic acid + 4 oxidized ferredoxin [iron-sulfur] cluster + 3 H2O | - |
? | |
27-hydroxycholest-4-en-3-one + 4 reduced ferredoxin [iron-sulfur] cluster + 4 H+ + O2 | Mycobacterium tuberculosis CDC 1551 | - |
cholest-4-en-3-one-27-oic acid + 4 oxidized ferredoxin [iron-sulfur] cluster + 3 H2O | - |
? | |
cholest-4-en-3-one + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 | Mycobacterium tuberculosis | physiological substrate, the enzyme hydroxylates cholest-4-en-3-one at C-27 | 27-hydroxycholest-4-en-3-one + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O | - |
? | |
cholest-4-en-3-one + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 | Mycobacterium tuberculosis CDC 1551 | physiological substrate, the enzyme hydroxylates cholest-4-en-3-one at C-27 | 27-hydroxycholest-4-en-3-one + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mycobacterium tuberculosis | P9WPP0 | - |
- |
Mycobacterium tuberculosis CDC 1551 | P9WPP0 | - |
- |
Purification (Comment) | Organism |
---|---|
- |
Mycobacterium tuberculosis |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
27-hydroxycholest-4-en-3-one + 4 reduced ferredoxin [iron-sulfur] cluster + 4 H+ + O2 | - |
Mycobacterium tuberculosis | cholest-4-en-3-one-27-oic acid + 4 oxidized ferredoxin [iron-sulfur] cluster + 3 H2O | - |
? | |
27-hydroxycholest-4-en-3-one + 4 reduced ferredoxin [iron-sulfur] cluster + 4 H+ + O2 | - |
Mycobacterium tuberculosis CDC 1551 | cholest-4-en-3-one-27-oic acid + 4 oxidized ferredoxin [iron-sulfur] cluster + 3 H2O | - |
? | |
cholest-4-en-3-one + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 | physiological substrate, the enzyme hydroxylates cholest-4-en-3-one at C-27 | Mycobacterium tuberculosis | 27-hydroxycholest-4-en-3-one + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O | - |
? | |
cholest-4-en-3-one + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 | physiological substrate, the enzyme hydroxylates cholest-4-en-3-one at C-27 | Mycobacterium tuberculosis CDC 1551 | 27-hydroxycholest-4-en-3-one + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O | - |
? |
Synonyms | Comment | Organism |
---|---|---|
CYP125A1 | - |
Mycobacterium tuberculosis |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NADPH | - |
Mycobacterium tuberculosis |
General Information | Comment | Organism |
---|---|---|
metabolism | CYP125A1 is a key enzyme in cholesterol metabolism and plays a crucial role in circumventing the deleterious effect of cholest-4-en-3-one | Mycobacterium tuberculosis |
physiological function | CYP125A1 is required to incorporate the cholesterol side chain carbon atoms into cellular lipids. CYP125A1 is essential for growth of CDC1551 in media containing cholesterol or cholest-4-en-3-one | Mycobacterium tuberculosis |