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Literature summary extracted from

  • Virus, C.; Lisurek, M.; Simgen, B.; Hannemann, F.; Bernhardt, R.
    Function and engineering of the 15beta-hydroxylase CYP106A2 (2006), Biochem. Soc. Trans., 34, 1215-1218.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.14.15.8 expression in Escherichia coli, wild type and mutant S72A/V73I, the DELTA72 mutant, which lacks the first 72 amino acids, is not expressed in Escherichia coli at a detectable amount, suggesting that the truncated mutant cannot fold properly within the bacterial cell Priestia megaterium

Protein Variants

EC Number Protein Variants Comment Organism
1.14.15.8 additional information modelling of CYP106A2 and site-directed mutagenesis of the protein to check the accuracy of the computer-derived model of CYP106A2 Priestia megaterium
1.14.15.8 S72A/V73I mutant does not show a better stability in the crystallization process than the wild-type protein Priestia megaterium

General Stability

EC Number General Stability Organism
1.14.15.8 by adding the ligands imidazole and metyrapone, it is not possible to prevent CYP106A2 from degradation in the crystallization process Priestia megaterium

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.14.15.8 47500
-
 x * 47500 Priestia megaterium

Organism

EC Number Organism UniProt Comment Textmining
1.14.15.8 Priestia megaterium Q06069 ATCC 13368
-

Storage Stability

EC Number Storage Stability Organism
1.14.15.8 4°C, 4 weeks, degradation during storage Priestia megaterium

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.15.8 additional information the specificity of hydroxylation in beta-position can be altered by the choice of the electron transfer system. Replacing the natural electron transfer partners by peroxides, the ratio of 15alpha-/15beta-hydroxylation of progesterone is increased 1.3fold Priestia megaterium ?
-
 ?
1.14.15.8 progesterone + reduced megaredoxin + O2
-
 Priestia megaterium 15beta-hydroxyprogesterone + oxidized megaredoxin + H2O
-
 ?
1.14.15.8 testosterone + reduced adrenodoxin + O2
-
 Priestia megaterium 15beta-hydroxytestosterone + oxidized adrenodoxin + H2O
-
 ?

Subunits

EC Number Subunits Comment Organism
1.14.15.8 ? x * 47500 Priestia megaterium

Synonyms

EC Number Synonyms Comment Organism
1.14.15.8 15beta-hydroxylase
-
 Priestia megaterium
1.14.15.8 CYP106A2
-
 Priestia megaterium

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.15.8 heme
-
 Priestia megaterium