Cloned (Comment) | Organism |
---|---|
- |
Mycobacterium tuberculosis |
Crystallization (Comment) | Organism |
---|---|
sitting drop method, the CYP142 crystal structure is solved to 1.6 A | Mycobacterium tuberculosis |
General Stability | Organism |
---|---|
completely to the P450 state on binding of cholest-4-en-3-one at pH 8.0 | Mycobacterium tuberculosis |
stabilizing effect of substrate binding on the thiolate-coordinated CYP142, to the extent that the P420 form of CYP142 can be converted almost | 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 | the enzyme can receive electrons from ferredoxin reductase in vitro, its natural electron donor is not known yet. The enzyme of the bacterial pathogen is involved degradation of the host cholesterol | (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 ATCC 25618 | the enzyme can receive electrons from ferredoxin reductase in vitro, its natural electron donor is not known yet. The enzyme of the bacterial pathogen is involved degradation of the host cholesterol | (25R)-3-oxocholest-4-en-26-oate + 6 oxidized [2Fe-2S] ferredoxin + 4 H2O | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mycobacterium tuberculosis | P9WPL5 | - |
- |
Mycobacterium tuberculosis ATCC 25618 | P9WPL5 | - |
- |
Purification (Comment) | Organism |
---|---|
- |
Mycobacterium tuberculosis |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
(25R)-26-hydroxycholest-4-en-3-one + 2 reduced [2Fe-2S] ferredoxin + O2 = (25R)-26-oxocholest-4-en-3-one + 2 oxidized [2Fe-2S] ferredoxin + 2 H2O | (1b) | Mycobacterium tuberculosis | |
(25R)-26-oxocholest-4-en-3-one + 2 reduced [2Fe-2S] ferredoxin + O2 = (25R)-3-oxocholest-4-en-26-oate + 2 oxidized [2Fe-2S] ferredoxin + H2O | (1c) | Mycobacterium tuberculosis | |
cholest-4-en-3-one + 2 reduced [2Fe-2S] ferredoxin + O2 = (25R)-26-hydroxycholest-4-en-3-one + 2 oxidized [2Fe-2S] ferredoxin + H2O | (1a) | Mycobacterium tuberculosis | |
cholest-4-en-3-one + 6 reduced [2Fe-2S] ferredoxin + 3 O2 = (25R)-3-oxocholest-4-en-26-oate + 6 oxidized [2Fe-2S] ferredoxin + 4 H2O | overall reaction | Mycobacterium tuberculosis |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
cholest-4-en-3-one + 6 reduced [2Fe-2S] ferredoxin + 3 O2 | the enzyme can receive electrons from ferredoxin reductase in vitro, its natural electron donor is not known yet. The enzyme of the bacterial pathogen is involved degradation of the host cholesterol | 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 | 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 | the enzyme can receive electrons from ferredoxin reductase in vitro, its natural electron donor is not known yet. The enzyme of the bacterial pathogen is involved degradation of the host cholesterol | Mycobacterium tuberculosis ATCC 25618 | (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 | 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 ATCC 25618 | (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 | - |
? | |
cholesterol + 6 reduced [2Fe-2S] ferredoxin + 3 O2 | - |
Mycobacterium tuberculosis ATCC 25618 | 3beta-hydroxycholest-5-en-26-oic acid + 6 oxidized [2Fe-2S] ferredoxin + 4 H2O | - |
? |
Synonyms | Comment | Organism |
---|---|---|
CYP142 | - |
Mycobacterium tuberculosis |
pH Stability | pH Stability Maximum | Comment | Organism |
---|---|---|---|
6 | - |
the substrate free enzyme is unstable and aggregates | Mycobacterium tuberculosis |
7 | - |
the P450 form of CYP142 is most stable at pH 7, and larger proportions of the P420 species are formed at the higher pH values, with near-complete P420 formation at pH 9 | Mycobacterium tuberculosis |
8 | - |
the spectrum for the Fe2+-CO form is notably unstable, and the P450 species progressively collapses over time with P420 accumulation | Mycobacterium tuberculosis |
General Information | Comment | Organism |
---|---|---|
metabolism | the enzyme is involved in host response modulation and cholesterol metabolism | Mycobacterium tuberculosis |