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

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

• Begley, Tadhg

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 2000

publisher

• Elsevier  Publisher

published in

• Bioorganic Chemistry  Journal

keywords

• 0601 Biochemistry And Cell Biology

PubMed Central ID

• 11133144

Digital Object Identifier (DOI)

• 10.1006/bioo.2000.1182

start page

• 261

end page

• 265

volume

• 28

issue

• 5

URL

• http%3A%2F%2Fdx.doi.org%2F10.1006%2Fbioo.2000.1182