Literature summary extracted from

Lamb, D.C.; Fowler, K.; Kieser, T.; Manning, N.; Podust, L.M.; Waterman, M.R.; Kelly, D.E.; Kelly, S.L.
Sterol 14alpha-demethylase activity in Streptomyces coelicolor A3(2) is associated with an unusual member of the CYP51 gene family (2002), Biochem. J., 364, 555-562.

Cloned(Commentary)

EC Number	Cloned (Comment)	Organism
1.14.14.154	expression in Escherichia coli with tetrahistidine tag	Streptomyces coelicolor

Protein Variants

EC Number	Protein Variants	Comment	Organism
1.14.14.154	additional information	mutant A3(2) containing a transposon insertion, no synthesis of functional hemoprotein, viable strain	Streptomyces coelicolor

Organism

EC Number	Organism	UniProt	Comment	Textmining
1.14.14.154	Streptomyces coelicolor	-	expression in Escherichia coli with tetrahistidine tag	-

Purification (Commentary)

EC Number	Purification (Comment)	Organism
1.14.14.154	recombinant enzyme	Streptomyces coelicolor

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
1.14.14.154	24-methylene-24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2	-	Streptomyces coelicolor	14alpha-demethyl-24-methylene-4alpha-methyl-5alpha-ergosta-8,14,24-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O	-	?
1.14.14.154	additional information	no substrate: lanosterol	Streptomyces coelicolor	?	-	?

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Release 2023.1 (January 2023)