Hydride Transfer Catalyzed by Glycerol Phosphate Dehydrogenase: Recruitment of an Acidic Amino Acid Side Chain to Rescue a Damaged Enzyme.

ABSTRACT: K120 of glycerol 3-phosphate dehydrogenase (GPDH) lies close to the carbonyl group of the bound dihydroxyacetone phosphate (DHAP) dianion. pH rate (pH 4.6-9.0) profiles are reported for k_cat and (k_cat/K_m)_dianion for wild type and K120A GPDH-catalyzed reduction of DHAP by NADH, and for (k_cat/K_dK_am) for activation of the variant-catalyzed reduction by CH₃CH₂NH₃⁺, where K_am and K_d are apparent dissociation constants for CH₃CH₂NH₃⁺ and DHAP, respectively. These profiles provide evidence that the K120 side chain cation, which is stabilized by an ion-pairin

SUBMITTER: He R 

PROVIDER: S-EPMC7784668 | biostudies-literature | 2020 Dec

REPOSITORIES: biostudies-literature