Mechanistic studies on prolyl-4-hydroxylase: The vitamin C requiring uncoupled oxidation

Authors
Wu, M Moon, HS Pirskanen, A Myllyharju, J Kivirikko, KI Begley, TP
Citation
M. Wu et al., Mechanistic studies on prolyl-4-hydroxylase: The vitamin C requiring uncoupled oxidation, BIOORG MED, 10(14), 2000, pp. 1511-1514
Citations number
17
Categorie Soggetti
Chemistry & Analysis
Journal title
BIOORGANIC & MEDICINAL CHEMISTRY LETTERS
ISSN journal
0960894X → ACNP
Volume
10
Issue
14
Year of publication
2000
Pages
1511 - 1514
Database
ISI
SICI code
0960-894X(20000717)10:14<1511:MSOPTV>2.0.ZU;2-X
Abstract
A deuteriated substrate for the human type I prolyl-4-hydroxylase was synth esized and its V/K deuterium isotope effect was determined to be 3.4 +/- 0. 2. This isotope effect was attributed to the uncoupled oxidation. A dehydro proline containing tetrapeptide was also found to stimulate the uncoupled o xidation. (C) 2000 Elsevier Science Ltd. All rights reserved.