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Literature summary extracted from

  • Capyk, J.; Kalscheuer, R.; Stewart, G.; Liu, J.; Kwon, H.; Zhao, R.; Okamoto, S.; Jacobs Jr., W.; Eltis, L.; Mohn, W.
    Mycobacterial cytochrome P450 125 (Cyp125) catalyzes the terminal hydroxylation of C27 steroids (2009), J. Biol. Chem., 284, 35534-35542.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) 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 Comment 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] Comment 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 UniProt Comment 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 Purification (Comment) 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 Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 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 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 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 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 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 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 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 Mycobacterium tuberculosis H37Rv 26-hydroxycholesterol + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.14.15.29 CYP125
-
 Mycobacterium tuberculosis
1.14.15.29 CYP125
-
 Mycobacterium tuberculosis variant bovis
1.14.15.29 cytochrome P450 125
-
 Mycobacterium tuberculosis
1.14.15.29 cytochrome P450 125
-
 Mycobacterium tuberculosis variant bovis
1.14.15.29 Rv3545c
-
 Mycobacterium tuberculosis
1.14.15.29 Rv3545c
-
 Mycobacterium tuberculosis variant bovis

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment 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 Comment Organism Structure
1.14.15.29 NADH
-
 Mycobacterium tuberculosis
1.14.15.29 NADH
-
 Mycobacterium tuberculosis variant bovis

Expression

EC Number Organism Comment 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 Comment Organism
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
1.14.15.29 physiological function Cyp125 is not essential for the growth of Mycobacterium tuberculosis on cholesterol Mycobacterium tuberculosis

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment 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