Literature summary for 1.14.15.22 extracted from

Hayashi, K.; Sugimoto, H.; Shinkyo, R.; Yamada, M.; Ikeda, S.; Ikushiro, S.; Kamakura, M.; Shiro, Y.; Sakaki, T.
Structure-based design of a highly active vitamin D hydroxylase from Streptomyces griseolus CYP105A1 (2008), Biochemistry, 47, 11964-11972.

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Protein Variants

Protein Variants	Comment	Organism
R73V/R84A	mutant exhibits 435- and 110fold higher kcat/Km values for the 25-hydroxylation of 1alpha-hydroxyvitamin D3 and 1alpha-hydroxylation of 25-hydroxyvitamin D3, respectively, compared with the wild-type	Streptomyces griseolus
R84F	mutation gives preference to the 1alpha-hydroxylation of 25-hydroxyvitamin D 3 over the 25-hydroxylation of 1alpha-hydroxyvitamin D 3, opposite to the wild type	Streptomyces griseolus

Organism

Organism	UniProt	Comment	Textmining
Streptomyces griseolus	P18326	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
1alpha-hydroxyvitamin D3 + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2	-	Streptomyces griseolus	1alpha,25-dihydroxyvitamin D3 + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O	-	?
25-hydroxyvitamin D3 + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2	-	Streptomyces griseolus	1alpha,25-dihydroxyvitamin D3 + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O	-	?
vitamin D3 + O2 + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+	-	Streptomyces griseolus	1alpha-hydroxyvitamin D3 + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O	-	?
vitamin D3 + O2 + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+	-	Streptomyces griseolus	25-hydroxyvitamin D3 + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O	-	?

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Release 2023.1 (January 2023)