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Use Of Di- And Tripropionate Substrate Analogs To Probe The Active Site Of Human Recombinant Coproporphyrinogen Oxidase, Justin B. Morgenthaler, Reyna L. Barto, Timothy D. Lash, Marjorie A. Jones

Faculty Publications – Chemistry

Background: Defects in the enzyme coproporphyrinogen oxidase result in accumulation of porphyrins which may affect the severity of a subset of porphyrias. Thus evaluation of this enzyme for substrate selectivity is of value. Kinetic evaluations of recombinant human coproporphyrinogen oxidase have been undertaken using six di- and tripropionate analogs of the natural substrate coproporphyrinogen-III. These Substrate analogs were modified by having alkyl groups in place of one or both of the ring 13- or 17-propionate moieties. Material/Methods: Cloned human enzyme was incubated with analogs under apparent first order conditions and with various substrate concentrations. The kinetic values, K-m and V-max, …