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Mechanistic studies on prolyl-4-hydroxylase: the vitamin C requiring uncoupled oxidation
1Department of Chemistry and Chemical Biology, Cornell University, Ithaca, NY 14853, USA.
Bioorganic & Medicinal Chemistry Letters
|July 29, 2000
Abstract:
A deuterated 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. This isotope effect was attributed to the uncoupled oxidation. A dehydroproline containing tetrapeptide was also found to stimulate the uncoupled oxidation.