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Kinetic Evaluation Of Human Cloned Coproporphyrinogen Oxidase Using A Ring Isomer Of The Natural Substrate, Marjorie A. Jones, Christopher L. Cooper, Timothy D. Lash
Kinetic Evaluation Of Human Cloned Coproporphyrinogen Oxidase Using A Ring Isomer Of The Natural Substrate, Marjorie A. Jones, Christopher L. Cooper, Timothy D. Lash
Faculty Publications – Chemistry
Background: The enzyme coproporphyrinogen oxidase (copro'gen oxidase) converts coproporphyrinogen-Ill (GIII) to protoporphyrinogen-IX via an intermediary monovinyl porphyrinogen. The A ring isomer coproporphyrinogen-IV (C-IV) has previously been shown to be a substrate for copro'gen oxidase derived from avian erythrocytes. In contrast to the authentic substrate (GIII) where only a small amount of the monovinyl intermediate is detected, C-IV gives rise to a monovinyl intermediate that accumulates before being converted to an isomer of protoporphyrinogen-IX. No kinetic studies have been carried out using the purified human copro'gen oxidase to evaluate its ability to process both the authentic substrate as well as analogs. …