title: Mechanistic Studies on Prolyl-4-Hydroxylase: Demonstration That the Ferryl Intermediate Does Not Exchange with Water.
abstract: Prolyl-4-hydroxylase catalyzes the formation of 4-hydroxyproline in collagens. In contrast to deacetoxy/deacetylcephalosporin C synthase, p-hydroxyphenylpyruvate hydroxylase, lysyl hydroxylase and alpha-ketoisocaproate oxygenase, no incorporation of (18)O-labeled water into the hydroxylated product was found for the human type I prolyl-4-hydroxylase when N-Cbz-Gly-L-Phe-L-Pro-Gly-OEt was used as a substrate. This suggests that the ferryl intermediate for this enzyme is not solvent accessible. Copyright 2000 Academic Press.
authors.affiliation: Department of Chemistry and Chemical Biology, Cornell University, Ithaca, New York, 14853
authors.initials: W
authors.lastname: Min
authors.initials: TP
authors.lastname: Begley
authors.initials: J
authors.lastname: Myllyharju
authors.initials: KI
authors.lastname: Kivirikko