Phosphodianion Activation of Enzymes for Catalysis of Central Metabolic Reactions.

ABSTRACT: The activation barriers ΔG^⧧ for k_cat/K_m for the reactions of whole substrates catalyzed by 6-phosphogluconate dehydrogenase, glucose 6-phosphate dehydrogenase, and glucose 6-phosphate isomerase are reduced by 11-13 kcal/mol by interactions between the protein and the substrate phosphodianion. Between 4 and 6 kcal/mol of this dianion binding energy is expressed at the transition state for phosphite dianion activation of the respective enzyme-catalyzed reactions of truncated substrates d-xylonate or d-xylose. These and earlier results from studies on β-phosphoglucomutase, triosephosphate isomerase, and glycerol 3-phosphate dehydrogenase define a cluster of six enzymes that catalyze reactions in glycolysis or of glycolytic intermediates, a

SUBMITTER: Fernandez PL 

PROVIDER: S-EPMC7919737 | biostudies-literature | 2021 Feb

REPOSITORIES: biostudies-literature