Mechanistic Studies on Prolyl-4-Hydroxylase: Demonstration That the Ferryl Intermediate Does Not Exchange with Water.
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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.
author list (cited authors)
Min, W., Begley, T. P., Myllyharju, J., & Kivirikko, K. I.
complete list of authors
Min, W||Begley, TP||Myllyharju, J||Kivirikko, KI