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Literature summary for 1.14.15.29 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
Search for more literature for 1.14.15.29

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Rhodococcus jostii strain RHA1 Mycobacterium tuberculosis
expressed in Rhodococcus jostii strain RHA1 Mycobacterium tuberculosis variant bovis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
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]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
46400
-
 MALDI-TOF mass spectrometry Mycobacterium tuberculosis
48200
-
 MALDI-TOF mass spectrometry Mycobacterium tuberculosis variant bovis

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis
-
-
-
Mycobacterium tuberculosis H37Rv
-
-
-
Mycobacterium tuberculosis variant bovis
-
-
-
Mycobacterium tuberculosis variant bovis bacillus Calmette-Guerin
-
-
-

Purification (Commentary)

Purification (Comment) Organism
Source 15Q column chromatography Mycobacterium tuberculosis
Source 15Q column chromatography Mycobacterium tuberculosis variant bovis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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
-
 ?
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
-
 ?
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
-
 ?
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
-
 ?
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
-
 ?
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
-
 ?
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
-
 ?
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

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

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
65
-
 the enzyme is heat inactivated by incubation at 65°C for 30 min Mycobacterium tuberculosis
65
-
 the enzyme is heat inactivated by incubation at 65°C for 30 min Mycobacterium tuberculosis variant bovis

Cofactor

Cofactor Comment Organism Structure
NADH
-
 Mycobacterium tuberculosis
NADH
-
 Mycobacterium tuberculosis variant bovis

Expression

Organism Comment Expression
Mycobacterium tuberculosis variant bovis cyp125 is up-regulated 7.1fold with growth on cholesterol up

General Information

General Information Comment Organism
physiological function Cyp125 is essential for the growth of Mycobacterium bovis strain bacillus Calmette-Guerin on cholesterol Mycobacterium tuberculosis variant bovis
physiological function Cyp125 is not essential for the growth of Mycobacterium tuberculosis on cholesterol Mycobacterium tuberculosis

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
11000
-
 O2 apparent value, in 0.1 M potassium phosphate at pH 7.0, temperature not specified in the publication Mycobacterium tuberculosis