Mechanistic Studies on Prolyl-4-Hydroxylase: Demonstration That the Ferryl Intermediate Does Not Exchange with Water. Academic Article uri icon


  • 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.

published proceedings

  • Bioorg Chem

author list (cited authors)

  • Min, W., Begley, T. P., Myllyharju, J., & Kivirikko, K. I.

citation count

  • 5

complete list of authors

  • Min, W||Begley, TP||Myllyharju, J||Kivirikko, KI

publication date

  • January 1, 2000 11:11 AM