Kinetic Studies of Novel Di- and Tri-propionate Substrates for the Chicken Red Blood Cell Enzyme Coproporphyrinogen Oxidase.

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概要

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• Coproporphyrinogen oxidase is an important enzyme in heme biosynthesis and catalyses the sequential oxidative decarboxylation of propionates on the A and B rings of the porphyrinogen ring. The effects of substituents on the C and D rings have not been systematically evaluated for their effects on the kinetic constants, Km and Vmax. A series of synthetic porphyrinogens have been tested for their ability to affect these kinetic constants for the chicken enzyme. The enzyme exhibited the largest Vmax when incubated with the authentic substrate and was clearly able to distinguish between various substituents on the C and D rings of the macrocycle. When co-incubated with substrate, the authentic product, protoporphyrinogen-IX, appears to inhibit coproporphyrinogen oxidase and this may have an important role in the regulation of this enzyme. Thus the model for the active site of this enzyme should be modified to take these factors into account

• 社団法人 日本生化学会の論文

著者

• HE J.

  Department of Chemistry, Illinois State University

• Jones M.

  Department Of Paediatric Surgery Alder Hey Children's Hospital

• Lash T.

  Department of Chemistry Illinois State University

関連論文

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• Kinetic Studies of Novel Di- and Tri-propionate Substrates for the Chicken Red Blood Cell Enzyme Coproporphyrinogen Oxidase.

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