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Investigation Of The Catalytic And Structural Roles Of Conserved Histidines Of Human Coproporphyrinogen Oxidase Using Site-Directed Mutagenesis, Shani J. Gitter, Christopher L. Cooper, Jon A. Frieson, Timothy D. Lash, Marjorie A. Jones
Investigation Of The Catalytic And Structural Roles Of Conserved Histidines Of Human Coproporphyrinogen Oxidase Using Site-Directed Mutagenesis, Shani J. Gitter, Christopher L. Cooper, Jon A. Frieson, Timothy D. Lash, Marjorie A. Jones
Faculty Publications – Chemistry
Background: The catalytic contribution of four conserved histidines of human coproporphyrinogen oxidase (CPO) has been investigated using site-directed mutagenesis to change histidine (H) into alanine (A). Material/Methods: The wild-type and mutant enzyme forms were analyzed for their ability to utilize coproporphyrinogen-III, mesoporphvrinogen-VI, and harderoporphyrinogen as substrates. Results: Wild-type CPO had specific activities of 4.9 +/- 0.9 nmole product/min/mg for coproporphyrinogen-III, 1.7 +/- 0.7 nmole ptoduct/min/mg for mesoporphyrinogen-VI, and 5.1 +/- 1.8 nmole product/min/mg for harderoporphyrinogen. The four mutant enzymes were catalytically competent With all three substrates, but to varying degrees. The most affected Mutant was the H158A enzyme which exhibited …