Literature summary for 1.14.15.8 extracted from

Janocha, S.; Carius, Y.; Hutter, M.; Lancaster, C.R.; Bernhardt, R.
Crystal structure of CYP106A2 in substrate-free and substrate-bound form (2016), ChemBioChem, 17, 852-860 .

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Crystallization (Commentary)

Crystallization (Comment)	Organism
substrate-free enzyme to 1.8 A resolution, cocrystallization of CYP106A2 with abietic acid reveals bending of the heme cofactor when abietic acid is bound in the active site	Priestia megaterium

Organism

Organism	UniProt	Comment	Textmining
Priestia megaterium	Q06069	isoform Cyp106A2	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
abietic acid + reduced adrenodoxin + O2	binding of abietic acid results in a type II difference spectrum typical for nitrogenous inhibitors	Priestia megaterium	? + oxidized adrenodoxin + H2O	-	?
dehydroabietic acid + reduced adrenodoxin + O2	-	Priestia megaterium	? + oxidized adrenodoxin + H2O	-	?
isopimaric acid + reduced adrenodoxin + O2	-	Priestia megaterium	? + oxidized adrenodoxin + H2O	-	?

Cofactor

Cofactor	Comment	Organism	Structure
heme	presence of dehydroabietic acid does not induce a high-spin shift of the enzyme	Priestia megaterium

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Release 2023.1 (January 2023)