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Literature summary for 1.14.15.28 extracted from

  • Johnston, J.B.; Ouellet, H.; Ortiz de Montellano, P.R.
    Functional redundancy of steroid C26-monooxygenase activity in Mycobacterium tuberculosis revealed by biochemical and genetic analyses (2010), J. Biol. Chem., 285, 36352-36360.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli Mycobacterium tuberculosis

KM Value [mM]

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/ Products (Substrates)

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

Organism UniProt Comment Textmining
Mycobacterium tuberculosis
-
-
-
Mycobacterium tuberculosis H37Rv
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Mycobacterium tuberculosis

Substrates and Products (Substrate)

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

Synonyms Comment Organism
CYP142A1
-
Mycobacterium tuberculosis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
21
-
assay at Mycobacterium tuberculosis

Turnover Number [1/s]

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

Cofactor Comment Organism Structure
cytochrome P450 cytochrome P450-dependent monooxygenase Mycobacterium tuberculosis

kcat/KM [mM/s]

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