BRENDA - Enzyme Database

Mycobacterial cytochrome P450 125 (Cyp125) catalyzes the terminal hydroxylation of C27 steroids

Capyk, J.; Kalscheuer, R.; Stewart, G.; Liu, J.; Kwon, H.; Zhao, R.; Okamoto, S.; Jacobs Jr., W.; Eltis, L.; Mohn, W.; J. Biol. Chem. 284, 35534-35542 (2009)

Data extracted from this reference:

Cloned(Commentary)
EC Number
Commentary
Organism
1.14.15.29
expressed in Rhodococcus jostii strain RHA1
Mycobacterium tuberculosis
1.14.15.29
expressed in Rhodococcus jostii strain RHA1
Mycobacterium tuberculosis variant bovis
KM Value [mM]
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
1.14.15.29
1.2
-
O2
apparent value, Km above 1.2 mM, in 0.1 M potassium phosphate at pH 7.0, temperature not specified in the publication
Mycobacterium tuberculosis
Molecular Weight [Da]
EC Number
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
1.14.15.29
46400
-
MALDI-TOF mass spectrometry
Mycobacterium tuberculosis
1.14.15.29
48200
-
MALDI-TOF mass spectrometry
Mycobacterium tuberculosis variant bovis
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
1.14.15.29
Mycobacterium tuberculosis
-
-
-
1.14.15.29
Mycobacterium tuberculosis H37Rv
-
-
-
1.14.15.29
Mycobacterium tuberculosis variant bovis
-
-
-
1.14.15.29
Mycobacterium tuberculosis variant bovis bacillus Calmette-Guerin
-
-
-
Purification (Commentary)
EC Number
Commentary
Organism
1.14.15.29
Source 15Q column chromatography
Mycobacterium tuberculosis
1.14.15.29
Source 15Q column chromatography
Mycobacterium tuberculosis variant bovis
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1.14.15.29
cholest-4-en-3-one + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
hydroxylation occurs at carbon 26 of the steroid side chain
717783
Mycobacterium tuberculosis
26-hydroxycholest-4-en-3-one + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
1.14.15.29
cholest-4-en-3-one + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
hydroxylation occurs at carbon 26 of the steroid side chain
717783
Mycobacterium tuberculosis variant bovis
26-hydroxycholest-4-en-3-one + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
1.14.15.29
cholest-4-en-3-one + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
hydroxylation occurs at carbon 26 of the steroid side chain
717783
Mycobacterium tuberculosis variant bovis bacillus Calmette-Guerin
26-hydroxycholest-4-en-3-one + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
1.14.15.29
cholest-4-en-3-one + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
hydroxylation occurs at carbon 26 of the steroid side chain
717783
Mycobacterium tuberculosis H37Rv
26-hydroxycholest-4-en-3-one + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
1.14.15.29
cholesterol + reduced ferredoxin [iron-sulfur] cluster + O2
hydroxylation occurs at carbon 26 of the steroid side chain
717783
Mycobacterium tuberculosis
26-hydroxycholesterol + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
1.14.15.29
cholesterol + reduced ferredoxin [iron-sulfur] cluster + O2
hydroxylation occurs at carbon 26 of the steroid side chain
717783
Mycobacterium tuberculosis variant bovis
26-hydroxycholesterol + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
1.14.15.29
cholesterol + reduced ferredoxin [iron-sulfur] cluster + O2
hydroxylation occurs at carbon 26 of the steroid side chain
717783
Mycobacterium tuberculosis variant bovis bacillus Calmette-Guerin
26-hydroxycholesterol + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
1.14.15.29
cholesterol + reduced ferredoxin [iron-sulfur] cluster + O2
hydroxylation occurs at carbon 26 of the steroid side chain
717783
Mycobacterium tuberculosis H37Rv
26-hydroxycholesterol + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
Temperature Stability [°C]
EC Number
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
1.14.15.29
65
-
the enzyme is heat inactivated by incubation at 65°C for 30 min
Mycobacterium tuberculosis
1.14.15.29
65
-
the enzyme is heat inactivated by incubation at 65°C for 30 min
Mycobacterium tuberculosis variant bovis
Cofactor
EC Number
Cofactor
Commentary
Organism
Structure
1.14.15.29
NADH
-
Mycobacterium tuberculosis variant bovis
1.14.15.29
NADH
-
Mycobacterium tuberculosis
Cloned(Commentary) (protein specific)
EC Number
Commentary
Organism
1.14.15.29
expressed in Rhodococcus jostii strain RHA1
Mycobacterium tuberculosis
1.14.15.29
expressed in Rhodococcus jostii strain RHA1
Mycobacterium tuberculosis variant bovis
Cofactor (protein specific)
EC Number
Cofactor
Commentary
Organism
Structure
1.14.15.29
NADH
-
Mycobacterium tuberculosis variant bovis
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
1.14.15.29
1.2
-
O2
apparent value, Km above 1.2 mM, in 0.1 M potassium phosphate at pH 7.0, temperature not specified in the publication
Mycobacterium tuberculosis
Molecular Weight [Da] (protein specific)
EC Number
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
1.14.15.29
46400
-
MALDI-TOF mass spectrometry
Mycobacterium tuberculosis
1.14.15.29
48200
-
MALDI-TOF mass spectrometry
Mycobacterium tuberculosis variant bovis
Purification (Commentary) (protein specific)
EC Number
Commentary
Organism
1.14.15.29
Source 15Q column chromatography
Mycobacterium tuberculosis
1.14.15.29
Source 15Q column chromatography
Mycobacterium tuberculosis variant bovis
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1.14.15.29
cholest-4-en-3-one + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
hydroxylation occurs at carbon 26 of the steroid side chain
717783
Mycobacterium tuberculosis
26-hydroxycholest-4-en-3-one + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
1.14.15.29
cholest-4-en-3-one + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
hydroxylation occurs at carbon 26 of the steroid side chain
717783
Mycobacterium tuberculosis variant bovis
26-hydroxycholest-4-en-3-one + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
1.14.15.29
cholest-4-en-3-one + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
hydroxylation occurs at carbon 26 of the steroid side chain
717783
Mycobacterium tuberculosis variant bovis bacillus Calmette-Guerin
26-hydroxycholest-4-en-3-one + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
1.14.15.29
cholest-4-en-3-one + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
hydroxylation occurs at carbon 26 of the steroid side chain
717783
Mycobacterium tuberculosis H37Rv
26-hydroxycholest-4-en-3-one + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
1.14.15.29
cholesterol + reduced ferredoxin [iron-sulfur] cluster + O2
hydroxylation occurs at carbon 26 of the steroid side chain
717783
Mycobacterium tuberculosis
26-hydroxycholesterol + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
1.14.15.29
cholesterol + reduced ferredoxin [iron-sulfur] cluster + O2
hydroxylation occurs at carbon 26 of the steroid side chain
717783
Mycobacterium tuberculosis variant bovis
26-hydroxycholesterol + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
1.14.15.29
cholesterol + reduced ferredoxin [iron-sulfur] cluster + O2
hydroxylation occurs at carbon 26 of the steroid side chain
717783
Mycobacterium tuberculosis variant bovis bacillus Calmette-Guerin
26-hydroxycholesterol + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
1.14.15.29
cholesterol + reduced ferredoxin [iron-sulfur] cluster + O2
hydroxylation occurs at carbon 26 of the steroid side chain
717783
Mycobacterium tuberculosis H37Rv
26-hydroxycholesterol + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
Temperature Stability [°C] (protein specific)
EC Number
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
1.14.15.29
65
-
the enzyme is heat inactivated by incubation at 65°C for 30 min
Mycobacterium tuberculosis
1.14.15.29
65
-
the enzyme is heat inactivated by incubation at 65°C for 30 min
Mycobacterium tuberculosis variant bovis
Expression
EC Number
Organism
Commentary
Expression
1.14.15.29
Mycobacterium tuberculosis variant bovis
cyp125 is up-regulated 7.1fold with growth on cholesterol
up
General Information
EC Number
General Information
Commentary
Organism
1.14.15.29
physiological function
Cyp125 is not essential for the growth of Mycobacterium tuberculosis on cholesterol
Mycobacterium tuberculosis
1.14.15.29
physiological function
Cyp125 is essential for the growth of Mycobacterium bovis strain bacillus Calmette-Guerin on cholesterol
Mycobacterium tuberculosis variant bovis
General Information (protein specific)
EC Number
General Information
Commentary
Organism
1.14.15.29
physiological function
Cyp125 is not essential for the growth of Mycobacterium tuberculosis on cholesterol
Mycobacterium tuberculosis
1.14.15.29
physiological function
Cyp125 is essential for the growth of Mycobacterium bovis strain bacillus Calmette-Guerin on cholesterol
Mycobacterium tuberculosis variant bovis
Expression (protein specific)
EC Number
Organism
Commentary
Expression
1.14.15.29
Mycobacterium tuberculosis variant bovis
cyp125 is up-regulated 7.1fold with growth on cholesterol
up
KCat/KM [mM/s]
EC Number
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
1.14.15.29
11000
-
O2
apparent value, in 0.1 M potassium phosphate at pH 7.0, temperature not specified in the publication
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
1.14.15.29
11000
-
O2
apparent value, in 0.1 M potassium phosphate at pH 7.0, temperature not specified in the publication
Mycobacterium tuberculosis