BRENDA - Enzyme Database

Functional redundancy of steroid C26-monooxygenase activity in Mycobacterium tuberculosis revealed by biochemical and genetic analyses

Johnston, J.B.; Ouellet, H.; Ortiz de Montellano, P.R.; J. Biol. Chem. 285, 36352-36360 (2010)

Data extracted from this reference:

Cloned(Commentary)
EC Number
Commentary
Organism
1.14.15.28
expressed in Escherichia coli
Mycobacterium tuberculosis
1.14.15.29
expressed in Escherichia coli
Mycobacterium tuberculosis
KM Value [mM]
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
1.14.15.28
0.0077
-
cholesterol
21°C, pH 7.4
Mycobacterium tuberculosis
1.14.15.28
0.0118
-
cholest-4-en-3-one
21°C, pH 7.4
Mycobacterium tuberculosis
1.14.15.29
0.0107
-
cholesterol
pH and temperature not specified in the publication
Mycobacterium tuberculosis
1.14.15.29
0.0208
-
cholest-4-en-3-one
pH and temperature not specified in the publication
Mycobacterium tuberculosis
Natural Substrates/ Products (Substrates)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
1.14.15.28
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
-
-
?
1.14.15.28
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
-
-
?
1.14.15.28
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
-
-
?
1.14.15.28
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
-
-
?
1.14.15.28
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
-
-
?
1.14.15.28
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
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
1.14.15.28
Mycobacterium tuberculosis
-
-
-
1.14.15.28
Mycobacterium tuberculosis H37Rv
-
-
-
1.14.15.29
Mycobacterium tuberculosis
-
-
-
1.14.15.29
Mycobacterium tuberculosis CDC 1551
-
-
-
1.14.15.29
Mycobacterium tuberculosis H37Rv
-
-
-
Purification (Commentary)
EC Number
Commentary
Organism
1.14.15.28
-
Mycobacterium tuberculosis
1.14.15.29
-
Mycobacterium tuberculosis
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1.14.15.28
(25R)-26-hydroxycholest-4-en-3-one + reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
-
717811
Mycobacterium tuberculosis
(25R)-26-oxocholest-4-en-3-one + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
1.14.15.28
(25R)-26-oxocholest-4-en-3-one + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
-
717811
Mycobacterium tuberculosis
(25R)-3-oxocholest-4-en-26-oate + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
1.14.15.28
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
717811
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 participates in cholesterol degradation
717811
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 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
717811
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
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
717811
Mycobacterium tuberculosis H37Rv
(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 participates in cholesterol degradation
717811
Mycobacterium tuberculosis H37Rv
(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 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
717811
Mycobacterium tuberculosis H37Rv
(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
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
717811
Mycobacterium tuberculosis CDC 1551
(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 participates in cholesterol degradation
717811
Mycobacterium tuberculosis CDC 1551
(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 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
717811
Mycobacterium tuberculosis CDC 1551
(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
-
717811
Mycobacterium tuberculosis
3beta-hydroxycholest-5-en-26-oic acid + 6 oxidized [2Fe-2S] ferredoxin + 4 H2O
-
-
-
?
1.14.15.29
cholest-4-en-3-one + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
-
717811
Mycobacterium tuberculosis
(25S)-26-hydroxycholest-4-en-3-one + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
CYP125A1 generates oxidized sterols of the (25S)-26-hydroxy configuration
-
-
?
1.14.15.29
cholest-4-en-3-one + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
-
717811
Mycobacterium tuberculosis H37Rv
(25S)-26-hydroxycholest-4-en-3-one + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
CYP125A1 generates oxidized sterols of the (25S)-26-hydroxy configuration
-
-
?
1.14.15.29
cholest-4-en-3-one + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
-
717811
Mycobacterium tuberculosis CDC 1551
(25S)-26-hydroxycholest-4-en-3-one + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
CYP125A1 generates oxidized sterols of the (25S)-26-hydroxy configuration
-
-
?
1.14.15.29
cholesterol + reduced ferredoxin [iron-sulfur] cluster + O2
-
717811
Mycobacterium tuberculosis
26-hydroxycholesterol + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
1.14.15.29
cholesterol + reduced ferredoxin [iron-sulfur] cluster + O2
-
717811
Mycobacterium tuberculosis H37Rv
26-hydroxycholesterol + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
1.14.15.29
cholesterol + reduced ferredoxin [iron-sulfur] cluster + O2
-
717811
Mycobacterium tuberculosis CDC 1551
26-hydroxycholesterol + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
Temperature Optimum [°C]
EC Number
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
1.14.15.28
21
-
assay at
Mycobacterium tuberculosis
Turnover Number [1/s]
EC Number
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
1.14.15.28
0.278
-
cholesterol
21°C, pH 7.4
Mycobacterium tuberculosis
1.14.15.28
1.4
-
cholest-4-en-3-one
21°C, pH 7.4
Mycobacterium tuberculosis
1.14.15.29
0.47
-
cholesterol
pH and temperature not specified in the publication
Mycobacterium tuberculosis
1.14.15.29
2.92
-
cholest-4-en-3-one
pH and temperature not specified in the publication
Mycobacterium tuberculosis
Cofactor
EC Number
Cofactor
Commentary
Organism
Structure
1.14.15.28
cytochrome P450
cytochrome P450-dependent monooxygenase
Mycobacterium tuberculosis
1.14.15.29
NADH
-
Mycobacterium tuberculosis
Cloned(Commentary) (protein specific)
EC Number
Commentary
Organism
1.14.15.28
expressed in Escherichia coli
Mycobacterium tuberculosis
1.14.15.29
expressed in Escherichia coli
Mycobacterium tuberculosis
Cofactor (protein specific)
EC Number
Cofactor
Commentary
Organism
Structure
1.14.15.28
cytochrome P450
cytochrome P450-dependent monooxygenase
Mycobacterium tuberculosis
1.14.15.29
NADH
-
Mycobacterium tuberculosis
KM Value [mM] (protein specific)
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
1.14.15.28
0.0077
-
cholesterol
21°C, pH 7.4
Mycobacterium tuberculosis
1.14.15.28
0.0118
-
cholest-4-en-3-one
21°C, pH 7.4
Mycobacterium tuberculosis
1.14.15.29
0.0107
-
cholesterol
pH and temperature not specified in the publication
Mycobacterium tuberculosis
1.14.15.29
0.0208
-
cholest-4-en-3-one
pH and temperature not specified in the publication
Mycobacterium tuberculosis
Natural Substrates/ Products (Substrates) (protein specific)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
1.14.15.28
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
-
-
?
1.14.15.28
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
-
-
?
1.14.15.28
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
-
-
?
1.14.15.28
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
-
-
?
1.14.15.28
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
-
-
?
1.14.15.28
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
-
-
?
Purification (Commentary) (protein specific)
EC Number
Commentary
Organism
1.14.15.28
-
Mycobacterium tuberculosis
1.14.15.29
-
Mycobacterium tuberculosis
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1.14.15.28
(25R)-26-hydroxycholest-4-en-3-one + reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
-
717811
Mycobacterium tuberculosis
(25R)-26-oxocholest-4-en-3-one + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
1.14.15.28
(25R)-26-oxocholest-4-en-3-one + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
-
717811
Mycobacterium tuberculosis
(25R)-3-oxocholest-4-en-26-oate + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
1.14.15.28
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
717811
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 participates in cholesterol degradation
717811
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 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
717811
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
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
717811
Mycobacterium tuberculosis H37Rv
(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 participates in cholesterol degradation
717811
Mycobacterium tuberculosis H37Rv
(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 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
717811
Mycobacterium tuberculosis H37Rv
(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
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
717811
Mycobacterium tuberculosis CDC 1551
(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 participates in cholesterol degradation
717811
Mycobacterium tuberculosis CDC 1551
(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 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
717811
Mycobacterium tuberculosis CDC 1551
(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
-
717811
Mycobacterium tuberculosis
3beta-hydroxycholest-5-en-26-oic acid + 6 oxidized [2Fe-2S] ferredoxin + 4 H2O
-
-
-
?
1.14.15.29
cholest-4-en-3-one + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
-
717811
Mycobacterium tuberculosis
(25S)-26-hydroxycholest-4-en-3-one + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
CYP125A1 generates oxidized sterols of the (25S)-26-hydroxy configuration
-
-
?
1.14.15.29
cholest-4-en-3-one + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
-
717811
Mycobacterium tuberculosis H37Rv
(25S)-26-hydroxycholest-4-en-3-one + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
CYP125A1 generates oxidized sterols of the (25S)-26-hydroxy configuration
-
-
?
1.14.15.29
cholest-4-en-3-one + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
-
717811
Mycobacterium tuberculosis CDC 1551
(25S)-26-hydroxycholest-4-en-3-one + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
CYP125A1 generates oxidized sterols of the (25S)-26-hydroxy configuration
-
-
?
1.14.15.29
cholesterol + reduced ferredoxin [iron-sulfur] cluster + O2
-
717811
Mycobacterium tuberculosis
26-hydroxycholesterol + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
1.14.15.29
cholesterol + reduced ferredoxin [iron-sulfur] cluster + O2
-
717811
Mycobacterium tuberculosis H37Rv
26-hydroxycholesterol + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
1.14.15.29
cholesterol + reduced ferredoxin [iron-sulfur] cluster + O2
-
717811
Mycobacterium tuberculosis CDC 1551
26-hydroxycholesterol + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
Temperature Optimum [°C] (protein specific)
EC Number
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
1.14.15.28
21
-
assay at
Mycobacterium tuberculosis
Turnover Number [1/s] (protein specific)
EC Number
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
1.14.15.28
0.278
-
cholesterol
21°C, pH 7.4
Mycobacterium tuberculosis
1.14.15.28
1.4
-
cholest-4-en-3-one
21°C, pH 7.4
Mycobacterium tuberculosis
1.14.15.29
0.47
-
cholesterol
pH and temperature not specified in the publication
Mycobacterium tuberculosis
1.14.15.29
2.92
-
cholest-4-en-3-one
pH and temperature not specified in the publication
Mycobacterium tuberculosis
KCat/KM [mM/s]
EC Number
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
1.14.15.28
36.1
-
cholesterol
21°C, pH 7.4
Mycobacterium tuberculosis
1.14.15.28
118.6
-
cholest-4-en-3-one
21°C, pH 7.4
Mycobacterium tuberculosis
KCat/KM [mM/s] (protein specific)
EC Number
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
1.14.15.28
36.1
-
cholesterol
21°C, pH 7.4
Mycobacterium tuberculosis
1.14.15.28
118.6
-
cholest-4-en-3-one
21°C, pH 7.4
Mycobacterium tuberculosis