297153-18-5Relevant academic research and scientific papers
Mechanistic Studies on Prolyl-4-Hydroxylase: Demonstration That the Ferryl Intermediate Does Not Exchange with Water
Wu, Min,Begley, Tadhg P.,Myllyharju, Johanna,Kivirikko, Kari I.
, p. 261 - 265 (2000)
Prolyl-4-hydroxylase catalyzes the formation of 4-hydroxyproline in collagens. In contrast to deacetoxy/deacetylcephalosporin C synthase, p-hydroxyphenylpyruvate hydroxylase, lysyl hydroxylase and α-ketoisocaproate oxygenase, no incorporation of 18O-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.
Mechanistic studies on prolyl-4-hydroxylase: The vitamin C requiring uncoupled oxidation
Wu, Min,Moon, Hong-sik,Pirskanen, Asta,Myllyharju, Johanna,Kivirikko, Kari I.,Begley, Tadhg P.
, p. 1511 - 1514 (2007/10/03)
A deuteriated substrate for the human type I prolyl-4-hydroxylase was synthesized and its V/K deuterium isotope effect was determined to be 3.4 ± 0.2. The isotope effect was attributed to the uncoupled oxidation. A dehydroproline containing tetrapeptide was also found to stimulate the uncoupled oxidation. (C) 2000 Elsevier Science Ltd. All rights reserved.
