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Literature summary extracted from

  • Zehentgruber, D.; Hannemann, F.; Bleif, S.; Bernhardt, R.; Lütz, S.
    Towards preparative scale steroid hydroxylation with cytochrome P450 monooxygenase CYP106A2. (2010), Chembiochem, 11, 713-721.
    View publication on PubMed

Application

EC Number Application Comment Organism
1.14.15.8 synthesis efficient approach towards the preparative scale synthesis of hydroxylated steroid derivatives. Improve CYP106A2-catalyzed steroid hydroxylation towards higher productivity and quantitative product formation. Because substrate transport into the cell limits the whole-cell biotransformation, activity can be increased sixfold by using membrane-free crude cell as biocatalyst Priestia megaterium

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.14.15.8 expression of the enzyme together with the electron-transfer partners bovine adrenodoxin and adrenodoxin reductase in Escherichia coli. Additionally an enzyme-coupled cofactor regeneration system was implemented by expressing alcohol dehydrogenase from Lactobacillus brevis. By studying the conversion of progesterone and testosterone, the bottlenecks of these P450-catalyzed hydroxylations are identified. Substrate transport into the cell and substrate solubility turned out to be crucial for the overall performance. Based on these investigations a new concept for CYP106A2-catalyzed steroid hydroxylations is developed by which the productivity of progesterone and testosterone conversion could be increased up to 18fold to yield an absolute productivity up to 5.5 g/L*d Priestia megaterium

Organism

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

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