Cloned (Comment) | Organism |
---|---|
expressed in Escherichia coli | Mycobacterium tuberculosis |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0077 | - |
cholesterol | 21°C, pH 7.4 | Mycobacterium tuberculosis | |
0.0118 | - |
cholest-4-en-3-one | 21°C, pH 7.4 | Mycobacterium tuberculosis |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
cholest-4-en-3-one + 6 reduced [2Fe-2S] ferredoxin + 3 O2 | Mycobacterium tuberculosis | dominant P450 enzyme responsible for initiating steroid side chain degradation in Mycobacterium tuberculosis. It is suggested that cholest-4-en-3-one rather than cholesterol is the most relevant in vivo substrate | (25R)-3-oxocholest-4-en-26-oate + 6 oxidized [2Fe-2S] ferredoxin + 4 H2O | - |
? | |
cholest-4-en-3-one + 6 reduced [2Fe-2S] ferredoxin + 3 O2 | Mycobacterium tuberculosis | the enzyme participates in cholesterol degradation | (25R)-3-oxocholest-4-en-26-oate + 6 oxidized [2Fe-2S] ferredoxin + 4 H2O | - |
? | |
cholest-4-en-3-one + 6 reduced [2Fe-2S] ferredoxin + 3 O2 | Mycobacterium tuberculosis H37Rv | dominant P450 enzyme responsible for initiating steroid side chain degradation in Mycobacterium tuberculosis. It is suggested that cholest-4-en-3-one rather than cholesterol is the most relevant in vivo substrate | (25R)-3-oxocholest-4-en-26-oate + 6 oxidized [2Fe-2S] ferredoxin + 4 H2O | - |
? | |
cholest-4-en-3-one + 6 reduced [2Fe-2S] ferredoxin + 3 O2 | Mycobacterium tuberculosis H37Rv | the enzyme participates in cholesterol degradation | (25R)-3-oxocholest-4-en-26-oate + 6 oxidized [2Fe-2S] ferredoxin + 4 H2O | - |
? | |
cholest-4-en-3-one + 6 reduced [2Fe-2S] ferredoxin + 3 O2 | Mycobacterium tuberculosis CDC 1551 | dominant P450 enzyme responsible for initiating steroid side chain degradation in Mycobacterium tuberculosis. It is suggested that cholest-4-en-3-one rather than cholesterol is the most relevant in vivo substrate | (25R)-3-oxocholest-4-en-26-oate + 6 oxidized [2Fe-2S] ferredoxin + 4 H2O | - |
? | |
cholest-4-en-3-one + 6 reduced [2Fe-2S] ferredoxin + 3 O2 | Mycobacterium tuberculosis CDC 1551 | the enzyme participates in cholesterol degradation | (25R)-3-oxocholest-4-en-26-oate + 6 oxidized [2Fe-2S] ferredoxin + 4 H2O | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mycobacterium tuberculosis | - |
- |
- |
Mycobacterium tuberculosis H37Rv | - |
- |
- |
Purification (Comment) | Organism |
---|---|
- |
Mycobacterium tuberculosis |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
(25R)-26-hydroxycholest-4-en-3-one + reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 | - |
Mycobacterium tuberculosis | (25R)-26-oxocholest-4-en-3-one + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O | - |
? | |
(25R)-26-oxocholest-4-en-3-one + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 | - |
Mycobacterium tuberculosis | (25R)-3-oxocholest-4-en-26-oate + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O | - |
? | |
cholest-4-en-3-one + 6 reduced [2Fe-2S] ferredoxin + 3 O2 | dominant P450 enzyme responsible for initiating steroid side chain degradation in Mycobacterium tuberculosis. It is suggested that cholest-4-en-3-one rather than cholesterol is the most relevant in vivo substrate | Mycobacterium tuberculosis | (25R)-3-oxocholest-4-en-26-oate + 6 oxidized [2Fe-2S] ferredoxin + 4 H2O | - |
? | |
cholest-4-en-3-one + 6 reduced [2Fe-2S] ferredoxin + 3 O2 | the enzyme participates in cholesterol degradation | Mycobacterium tuberculosis | (25R)-3-oxocholest-4-en-26-oate + 6 oxidized [2Fe-2S] ferredoxin + 4 H2O | - |
? | |
cholest-4-en-3-one + 6 reduced [2Fe-2S] ferredoxin + 3 O2 | the enzyme catalyses the hydroxylation of the C-26 carbon, followed by oxidation of the alcohol to the carboxylic acid via the aldehyde intermediate, initiating the degradation of the alkyl side-chain of cholesterol. The products are exclusively in the (25R) conformation | Mycobacterium tuberculosis | (25R)-3-oxocholest-4-en-26-oate + 6 oxidized [2Fe-2S] ferredoxin + 4 H2O | - |
? | |
cholest-4-en-3-one + 6 reduced [2Fe-2S] ferredoxin + 3 O2 | dominant P450 enzyme responsible for initiating steroid side chain degradation in Mycobacterium tuberculosis. It is suggested that cholest-4-en-3-one rather than cholesterol is the most relevant in vivo substrate | Mycobacterium tuberculosis H37Rv | (25R)-3-oxocholest-4-en-26-oate + 6 oxidized [2Fe-2S] ferredoxin + 4 H2O | - |
? | |
cholest-4-en-3-one + 6 reduced [2Fe-2S] ferredoxin + 3 O2 | the enzyme participates in cholesterol degradation | Mycobacterium tuberculosis H37Rv | (25R)-3-oxocholest-4-en-26-oate + 6 oxidized [2Fe-2S] ferredoxin + 4 H2O | - |
? | |
cholest-4-en-3-one + 6 reduced [2Fe-2S] ferredoxin + 3 O2 | the enzyme catalyses the hydroxylation of the C-26 carbon, followed by oxidation of the alcohol to the carboxylic acid via the aldehyde intermediate, initiating the degradation of the alkyl side-chain of cholesterol. The products are exclusively in the (25R) conformation | Mycobacterium tuberculosis H37Rv | (25R)-3-oxocholest-4-en-26-oate + 6 oxidized [2Fe-2S] ferredoxin + 4 H2O | - |
? | |
cholest-4-en-3-one + 6 reduced [2Fe-2S] ferredoxin + 3 O2 | dominant P450 enzyme responsible for initiating steroid side chain degradation in Mycobacterium tuberculosis. It is suggested that cholest-4-en-3-one rather than cholesterol is the most relevant in vivo substrate | Mycobacterium tuberculosis CDC 1551 | (25R)-3-oxocholest-4-en-26-oate + 6 oxidized [2Fe-2S] ferredoxin + 4 H2O | - |
? | |
cholest-4-en-3-one + 6 reduced [2Fe-2S] ferredoxin + 3 O2 | the enzyme participates in cholesterol degradation | Mycobacterium tuberculosis CDC 1551 | (25R)-3-oxocholest-4-en-26-oate + 6 oxidized [2Fe-2S] ferredoxin + 4 H2O | - |
? | |
cholest-4-en-3-one + 6 reduced [2Fe-2S] ferredoxin + 3 O2 | the enzyme catalyses the hydroxylation of the C-26 carbon, followed by oxidation of the alcohol to the carboxylic acid via the aldehyde intermediate, initiating the degradation of the alkyl side-chain of cholesterol. The products are exclusively in the (25R) conformation | Mycobacterium tuberculosis CDC 1551 | (25R)-3-oxocholest-4-en-26-oate + 6 oxidized [2Fe-2S] ferredoxin + 4 H2O | - |
? | |
cholesterol + 6 reduced [2Fe-2S] ferredoxin + 3 O2 | - |
Mycobacterium tuberculosis | 3beta-hydroxycholest-5-en-26-oic acid + 6 oxidized [2Fe-2S] ferredoxin + 4 H2O | - |
? |
Synonyms | Comment | Organism |
---|---|---|
CYP142A1 | - |
Mycobacterium tuberculosis |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
21 | - |
assay at | Mycobacterium tuberculosis |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.278 | - |
cholesterol | 21°C, pH 7.4 | Mycobacterium tuberculosis | |
1.4 | - |
cholest-4-en-3-one | 21°C, pH 7.4 | Mycobacterium tuberculosis |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
cytochrome P450 | cytochrome P450-dependent monooxygenase | Mycobacterium tuberculosis |
kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
36.1 | - |
cholesterol | 21°C, pH 7.4 | Mycobacterium tuberculosis | |
118.6 | - |
cholest-4-en-3-one | 21°C, pH 7.4 | Mycobacterium tuberculosis |