Literature summary for 1.14.15.8 extracted from

Rauschenbach, R.; Isernhagen, M.; Noeske-Jungblut, C.; Boidol, W.; Siewert, G.
Cloning sequencing and expression of the gene for cytochrome P450meg, the steroid-15 beta-monooxygenase from Bacillus megaterium ATCC 13368 (1993), Mol. Gen. Genet., 241, 170-176.

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Cloned(Commentary)

Cloned (Comment)	Organism
expressed in Escherichia coli and Bacillus subtilis. No hydroxylation is found with protein extracts from recombinant Escherichia coli strains since cytochrome P450meg needs additional electron transfer proteins for enzymatic activity, which are missing in Escherichia coli. Bacillus subtilis, in contrast to Escherichia coli, contains an electron transfer system capable of supporting the activity of cytochrome P450meg	Priestia megaterium

Cloned (Comment)

Organism

expressed in Escherichia coli and Bacillus subtilis. No hydroxylation is found with protein extracts from recombinant Escherichia coli strains since cytochrome P450meg needs additional electron transfer proteins for enzymatic activity, which are missing in Escherichia coli. Bacillus subtilis, in contrast to Escherichia coli, contains an electron transfer system capable of supporting the activity of cytochrome P450meg

Priestia megaterium

Organism

Organism	UniProt	Comment	Textmining
Priestia megaterium	Q06069	ATCC 13368	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
6alpha-fluoro-16alpha-methyl-deoxycorticosterone + reduced ferredoxin + O2	-	Priestia megaterium	15beta-hydroxy-6alpha-fluoro-16alpha-methyl-deoxycorticosterone + oxidized ferredoxin + H2O	-	?

Synonyms

Synonyms	Comment	Organism
cytochrome P450meg	-	Priestia megaterium
steroid-15-beta-monooxygenase	-	Priestia megaterium

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Release 2023.1 (January 2023)