Literature summary for 1.14.15.8 extracted from

Zehentgruber, D.; Hannemann, F.; Bleif, S.; Bernhardt, R.; L�tz, S.
Towards preparative scale steroid hydroxylation with cytochrome P450 monooxygenase CYP106A2. (2010), Chembiochem, 11, 713-721.

Search for more literature for 1.14.15.8

Application

Application	Comment	Organism
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)

Cloned (Comment)	Organism
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

Cloned (Comment)

Organism

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

Organism	UniProt	Comment	Textmining
Priestia megaterium	Q06069	ATCC 13368	-

Synonyms

Synonyms	Comment	Organism
15beta-hydroxylase CYP106A2	-	Priestia megaterium
CYP106A2	-	Priestia megaterium

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Release 2023.1 (January 2023)