Literature summary for 1.14.15.8 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.

Search for more literature for 1.14.15.8

Cloned(Commentary)

Cloned (Comment)	Organism
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

Protein Variants	Comment	Organism
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
S72A/V73I	mutant does not show a better stability in the crystallization process than the wild-type protein	Priestia megaterium

General Stability

General Stability	Organism
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]

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

Organism

Organism	UniProt	Comment	Textmining
Priestia megaterium	Q06069	ATCC 13368	-

Storage Stability

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

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
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	?	-	?
progesterone + reduced megaredoxin + O2	-	Priestia megaterium	15beta-hydroxyprogesterone + oxidized megaredoxin + H2O	-	?
testosterone + reduced adrenodoxin + O2	-	Priestia megaterium	15beta-hydroxytestosterone + oxidized adrenodoxin + H2O	-	?

Subunits

Subunits	Comment	Organism
?	x * 47500	Priestia megaterium

Synonyms

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

Cofactor

Cofactor	Comment	Organism	Structure
heme	-	Priestia megaterium

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Release 2023.1 (January 2023)