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

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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.

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xi, 132 leaves : ill.

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Berdis, Anthony J. (Anthony Joseph) May 1993.

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  • Berdis, Anthony J. (Anthony Joseph)

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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.

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xi, 132 leaves : ill.

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  • May 1993

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  • March 24, 2014, 8:07 p.m.

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  • Feb. 19, 2015, 10:17 a.m.

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Berdis, Anthony J. (Anthony Joseph). Kinetic and Chemical Mechanism of 6-phosphogluconate Dehydrogenase from Candida Utilis, dissertation, May 1993; Denton, Texas. (digital.library.unt.edu/ark:/67531/metadc278323/: accessed November 24, 2017), University of North Texas Libraries, Digital Library, digital.library.unt.edu; .