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Literature summary extracted from

  • Driscoll, M.D.; McLean, K.J.; Levy, C.; Mast, N.; Pikuleva, I.A.; Lafite, P.; Rigby, S.E.; Leys, D.; Munro, A.W.
    Structural and biochemical characterization of Mycobacterium tuberculosis CYP142: evidence for multiple cholesterol 27-hydroxylase activities in a human pathogen (2010), J. Biol. Chem., 285, 38270-38282.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.14.15.28
-
 Mycobacterium tuberculosis

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.14.15.28 sitting drop method, the CYP142 crystal structure is solved to 1.6 A Mycobacterium tuberculosis

General Stability

EC Number General Stability Organism
1.14.15.28 completely to the P450 state on binding of cholest-4-en-3-one at pH 8.0 Mycobacterium tuberculosis
1.14.15.28 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/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.14.15.28 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
-
 ?
1.14.15.28 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

EC Number Organism UniProt Comment Textmining
1.14.15.28 Mycobacterium tuberculosis P9WPL5
-
-
1.14.15.28 Mycobacterium tuberculosis ATCC 25618 P9WPL5
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.14.15.28
-
 Mycobacterium tuberculosis

Reaction

EC Number Reaction Comment Organism Reaction ID
1.14.15.28 (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
a
1.14.15.28 (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
a
1.14.15.28 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
a
1.14.15.28 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
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.15.28 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
-
 ?
1.14.15.28 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
-
 ?
1.14.15.28 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
-
 ?
1.14.15.28 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
-
 ?
1.14.15.28 cholesterol + 6 reduced [2Fe-2S] ferredoxin + 3 O2
-
 Mycobacterium tuberculosis 3beta-hydroxycholest-5-en-26-oic acid + 6 oxidized [2Fe-2S] ferredoxin + 4 H2O
-
 ?
1.14.15.28 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

EC Number Synonyms Comment Organism
1.14.15.28 CYP142
-
 Mycobacterium tuberculosis

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
1.14.15.28 6
-
 the substrate free enzyme is unstable and aggregates Mycobacterium tuberculosis
1.14.15.28 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
1.14.15.28 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

EC Number General Information Comment Organism
1.14.15.28 metabolism the enzyme is involved in host response modulation and cholesterol metabolism Mycobacterium tuberculosis