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The Organization of Active Site Side Chains of Glycerol-3-phosphate Dehydrogenase Promotes Efficient Enzyme Catalysis and Rescue of Variant Enzymes.

Biochemistry - 28 Apr 2020

Cristobal Judith R, Reyes Archie C, Richard John P

Abstract excerpt

A comparison of the values of kcat/Km for reduction of dihydroxyacetone phosphate (DHAP) by NADH catalyzed by wild type and K120A/R269A variant glycerol-3-phosphate dehydrogenase from human liver (hlGPDH) shows that the transition state for enzyme-catalyzed hydride transfer is stabilized by 12.0 kcal/mol by interactions with the cationic K120 and R269 side chains. The transition state for the K120A/R269A...

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Identifiers

PMID: 32250105
DOI: 10.1021/acs.biochem.0c00175
PMCID: PMC7207223

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