Mechanistic studies on prolyl-4-hydroxylase: the vitamin c requiring uncoupled oxidation

Mechanistic studies on prolyl-4-hydroxylase: the vitamin c requiring uncoupled oxidation

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. This isotope effect was attributed to the uncoupled oxidation. A dehydroproline containing tetrapeptide was also found to stimulate the uncoupled oxi...

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Veröffentlicht in:Bioorganic & medicinal chemistry letters 2000-07, Vol.10 (14), p.1511-1514
Hauptverfasser: Wu, Min, Moon, Hong-sik, Pirskanen, Asta, Myllyharju, Johanna, Kivirikko, Kari I., Begley, Tadhg P.
Format: Artikel
Sprache:eng
Schlagworte:
Amino Acid Sequence
Analytical, structural and metabolic biochemistry
Ascorbic Acid - metabolism
Biological and medical sciences
Deuterium
Enzymes and enzyme inhibitors
Fundamental and applied biological sciences. Psychology
Humans
Kinetics
Oligopeptides - chemical synthesis
Oligopeptides - chemistry
Oligopeptides - metabolism
Oxidation-Reduction
Oxidoreductases
Procollagen - chemistry
Procollagen - metabolism
Procollagen-Proline Dioxygenase - metabolism
Proline
Substrate Specificity
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Zusammenfassung: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. This isotope effect was attributed to the uncoupled oxidation. A dehydroproline containing tetrapeptide was also found to stimulate the uncoupled oxidation.
ISSN:0960-894X
1464-3405
DOI:10.1016/S0960-894X(00)00224-9