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Kinetic and Chemical Mechanism of 6-phosphogluconate Dehydrogenase from Candida Utilis

A complete initial velocity study of the 6-phosphogluconate dehydrogenase from Candida utilis in both reaction directions suggests a rapid equilibrium random kinetic mechanism with dead-end E:NADP:(ribulose 5-phosphate) and E:NADPH:(6- phosphogluconate) complexes. Initial velocity studies obtained as a function of pH and using NAD as the dinucleotide substrate for the reaction suggest that the 2'-phosphate is critical for productive binding of the dinucleotide substrate. Primary deuterium isotope effects using 3-<i-6-phosphogluconate were obtained for the 6-phosphogluconate dehydrogenase reaction using NADP and various alternative inucleotide substrates.

Identiferoai:union.ndltd.org:unt.edu/info:ark/67531/metadc278323
Date05 1900
CreatorsBerdis, Anthony J. (Anthony Joseph)
ContributorsCook, Paul F., Harris, Ben G., Gracy, Robert W., Hall, James, Alvarez-Gonzalez, Rafael
PublisherUniversity of North Texas
Source SetsUniversity of North Texas
LanguageEnglish
Detected LanguageEnglish
TypeThesis or Dissertation
Formatxi, 132 leaves : ill., Text
RightsPublic, Copyright, Copyright is held by the author, unless otherwise noted. All rights reserved., Berdis, Anthony J. (Anthony Joseph)

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