Literature summary for 1.14.19.69 extracted from

Zhao, B.; Guengerich, F.P.; Bellamine, A.; Lamb, D.C.; Izumikawa, M.; Lei, L.; Podust, L.M.; Sundaramoorthy, M.; Kalaitzis, J.A.; Reddy, L.M.; Kelly, S.L.; Moore, B.S.; Stec, D.; Voehler, M.; Falck, J.R.; Shimada, T.; Waterman, M.R.
Binding of two flaviolin substrate molecules, oxidative coupling, and crystal structure of Streptomyces coelicolor A3(2) cytochrome P450 158A2 (2005), J. Biol. Chem., 280, 11599-11607.

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Cloned(Commentary)

Cloned (Comment)	Organism
-	Streptomyces coelicolor

Crystallization (Commentary)

Crystallization (Comment)	Organism
free enzyme and in complex with flaviolin, diffration to 1.75 and 1.62 A resolution, respectively.Upon ligand binding, a major conformational change takes place that closes the entry into the active site, partly due to repositioning of the F and G helices. Presence of two molecules of flaviolin in the closed active site that form a quasi-planar three-molecule stack including the heme	Streptomyces coelicolor

Organism

Organism	UniProt	Comment	Textmining
Streptomyces coelicolor	-	isoform CYP158A2	-
Streptomyces coelicolor A3(2)	-	isoform CYP158A2	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant protein	Streptomyces coelicolor

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
4 flaviolin + 4 reduced ferredoxin [iron-sulfur] cluster + 4 H+ + O2	-	Streptomyces coelicolor	3,3'-biflaviolin + 3,8'-biflaviolin + 4 oxidized ferredoxin [iron-sulfur] cluster + 4 H2O	plus some further biflaviolin isomer and some triflaviolin	?
4 flaviolin + 4 reduced ferredoxin [iron-sulfur] cluster + 4 H+ + O2	-	Streptomyces coelicolor A3(2)	3,3'-biflaviolin + 3,8'-biflaviolin + 4 oxidized ferredoxin [iron-sulfur] cluster + 4 H2O	plus some further biflaviolin isomer and some triflaviolin	?

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
0.017	-	flaviolin	pH 7.5, 37°C	Streptomyces coelicolor

Cofactor

Cofactor	Comment	Organism	Structure
cytochrome P450	-	Streptomyces coelicolor
heme	-	Streptomyces coelicolor

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Release 2023.1 (January 2023)