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(25R)-25-bromo-27-norcholesterol + 6 reduced [2Fe-2S] ferredoxin + 3 O2
(25R)-25-bromo-27-norcholesterol-26-oate + 6 oxidized [2Fe-2S] ferredoxin + 4 H2O
(25R)-26-hydroxycholest-4-en-3-one + reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
(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
(25R)-3-oxocholest-4-en-26-oate + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
-
?
26-methylcholesterol + 6 reduced [2Fe-2S] ferredoxin + 3 O2
(25R)-3beta-hydroxycholest-5-en-27-oate + 6 oxidized [2Fe-2S] ferredoxin + 4 H2O
cholest-4-en-3-one + 6 reduced [2Fe-2S] ferredoxin
(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
(25R)-3-oxocholest-4-en-26-oate + 6 oxidized [2Fe-2S] ferredoxin + 4 H2O
cholest-5-en-3-beta-ol + 6 reduced [2Fe-2S] ferredoxin + 3 O2
(25R)-3beta-hydroxycholest-5-en-26-oate + 6 oxidized [2Fe-2S] ferredoxin + 4 H2O
cholesterol + 6 reduced [2Fe-2S] ferredoxin + 3 O2
3beta-hydroxycholest-5-en-26-oic acid + 6 oxidized [2Fe-2S] ferredoxin + 4 H2O
lanosterol + 6 reduced [2Fe-2S] ferredoxin + 3 O2
lanosterol-26-oate + 6 oxidized [2Fe-2S] ferredoxin + 4 H2O
additional information
?
-
(25R)-25-bromo-27-norcholesterol + 6 reduced [2Fe-2S] ferredoxin + 3 O2
(25R)-25-bromo-27-norcholesterol-26-oate + 6 oxidized [2Fe-2S] ferredoxin + 4 H2O
-
-
-
?
(25R)-25-bromo-27-norcholesterol + 6 reduced [2Fe-2S] ferredoxin + 3 O2
(25R)-25-bromo-27-norcholesterol-26-oate + 6 oxidized [2Fe-2S] ferredoxin + 4 H2O
-
-
-
?
26-methylcholesterol + 6 reduced [2Fe-2S] ferredoxin + 3 O2
(25R)-3beta-hydroxycholest-5-en-27-oate + 6 oxidized [2Fe-2S] ferredoxin + 4 H2O
-
-
-
?
26-methylcholesterol + 6 reduced [2Fe-2S] ferredoxin + 3 O2
(25R)-3beta-hydroxycholest-5-en-27-oate + 6 oxidized [2Fe-2S] ferredoxin + 4 H2O
-
-
-
?
cholest-4-en-3-one + 6 reduced [2Fe-2S] ferredoxin
(25R)-3-oxocholest-4-en-26-oate + 6 oxidized [2Fe-2S] ferredoxin + 4 H2O
-
-
-
-
?
cholest-4-en-3-one + 6 reduced [2Fe-2S] ferredoxin
(25R)-3-oxocholest-4-en-26-oate + 6 oxidized [2Fe-2S] ferredoxin + 4 H2O
-
-
-
?
cholest-4-en-3-one + 6 reduced [2Fe-2S] ferredoxin
(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
(25R)-3-oxocholest-4-en-26-oate + 6 oxidized [2Fe-2S] ferredoxin + 4 H2O
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
-
-
?
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
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
-
-
?
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
-
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
-
-
?
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
-
the enzyme participates in cholesterol degradation
-
-
?
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
-
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
-
-
?
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
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
-
-
?
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
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
-
-
?
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
-
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
-
-
?
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
-
the enzyme participates in cholesterol degradation
-
-
?
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
-
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
-
-
?
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
-
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
-
-
?
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
-
the enzyme participates in cholesterol degradation
-
-
?
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
-
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
-
-
?
cholest-5-en-3-beta-ol + 6 reduced [2Fe-2S] ferredoxin + 3 O2
(25R)-3beta-hydroxycholest-5-en-26-oate + 6 oxidized [2Fe-2S] ferredoxin + 4 H2O
-
-
-
?
cholest-5-en-3-beta-ol + 6 reduced [2Fe-2S] ferredoxin + 3 O2
(25R)-3beta-hydroxycholest-5-en-26-oate + 6 oxidized [2Fe-2S] ferredoxin + 4 H2O
-
-
-
?
cholesterol + 6 reduced [2Fe-2S] ferredoxin + 3 O2
3beta-hydroxycholest-5-en-26-oic acid + 6 oxidized [2Fe-2S] ferredoxin + 4 H2O
-
-
-
-
?
cholesterol + 6 reduced [2Fe-2S] ferredoxin + 3 O2
3beta-hydroxycholest-5-en-26-oic acid + 6 oxidized [2Fe-2S] ferredoxin + 4 H2O
-
-
-
?
cholesterol + 6 reduced [2Fe-2S] ferredoxin + 3 O2
3beta-hydroxycholest-5-en-26-oic acid + 6 oxidized [2Fe-2S] ferredoxin + 4 H2O
-
-
-
?
lanosterol + 6 reduced [2Fe-2S] ferredoxin + 3 O2
lanosterol-26-oate + 6 oxidized [2Fe-2S] ferredoxin + 4 H2O
-
-
-
?
lanosterol + 6 reduced [2Fe-2S] ferredoxin + 3 O2
lanosterol-26-oate + 6 oxidized [2Fe-2S] ferredoxin + 4 H2O
-
-
-
?
additional information
?
-
no substrates: 25-thia-27-norcholesterol, 24-bromochol-5-enol, 26-methylcholesta-5,25(26)-dienol
-
-
?
additional information
?
-
-
no substrates: 25-thia-27-norcholesterol, 24-bromochol-5-enol, 26-methylcholesta-5,25(26)-dienol
-
-
?
additional information
?
-
no substrates: 25-thia-27-norcholesterol, 24-bromochol-5-enol, 26-methylcholesta-5,25(26)-dienol
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
cholest-4-en-3-one + 6 reduced [2Fe-2S] ferredoxin
(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
(25R)-3-oxocholest-4-en-26-oate + 6 oxidized [2Fe-2S] ferredoxin + 4 H2O
cholest-4-en-3-one + 6 reduced [2Fe-2S] ferredoxin
(25R)-3-oxocholest-4-en-26-oate + 6 oxidized [2Fe-2S] ferredoxin + 4 H2O
-
-
-
-
?
cholest-4-en-3-one + 6 reduced [2Fe-2S] ferredoxin
(25R)-3-oxocholest-4-en-26-oate + 6 oxidized [2Fe-2S] ferredoxin + 4 H2O
-
-
-
?
cholest-4-en-3-one + 6 reduced [2Fe-2S] ferredoxin
(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
(25R)-3-oxocholest-4-en-26-oate + 6 oxidized [2Fe-2S] ferredoxin + 4 H2O
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
-
-
?
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
-
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
-
-
?
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
-
the enzyme participates in cholesterol degradation
-
-
?
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
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
-
-
?
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
-
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
-
-
?
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
-
the enzyme participates in cholesterol degradation
-
-
?
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
-
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
-
-
?
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
-
the enzyme participates in cholesterol degradation
-
-
?
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Ouellet, H.; Lang, J.; Couture, M.; De Montellano, P.
Reaction of Mycobacterium tuberculosis Cytochrome P450 enzymes with nitric oxide
Biochemistry
48
863-872
2009
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
brenda
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
J. Biol. Chem.
285
36352-36360
2010
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
brenda
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
J. Biol. Chem.
285
38270-38282
2010
Mycobacterium tuberculosis (P9WPL5), Mycobacterium tuberculosis, Mycobacterium tuberculosis ATCC 25618 (P9WPL5)
brenda
Garcia-Fernandez, E.; Frank, D.J.; Galan, B.; Kells, P.M.; Podust, L.M.; Garcia, J.L.; Ortiz de Montellano, P.R.
A highly conserved mycobacterial cholesterol catabolic pathway
Environ. Microbiol.
15
2342-2359
2013
Mycolicibacterium smegmatis, Mycolicibacterium smegmatis mc(2)155
brenda
Frank, D.J.; Madrona, Y.; Ortiz de Montellano, P.R.
Cholesterol ester oxidation by mycobacterial cytochrome P450
J. Biol. Chem.
289
30417-30425
2014
Mycolicibacterium smegmatis (A0R4Q6)
brenda
Johnston, J.B.; Singh, A.A.; Clary, A.A.; Chen, C.K.; Hayes, P.Y.; Chow, S.; De Voss, J.J.; Ortiz de Montellano, P.R.
Substrate analog studies of the omega-regiospecificity of Mycobacterium tuberculosis cholesterol metabolizing cytochrome P450 enzymes CYP124A1, CYP125A1 and CYP142A1
Bioorg. Med. Chem.
20
4064-4081
2012
Mycobacterium tuberculosis (P9WPL5), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WPL5)
brenda