Modeling the Role of a Flexible Loop and Active Site Side Chains in Hydride Transfer Catalyzed by Glycerol-3-phosphate Dehydrogenase

• Published in: ACS catalysis Vol. 10; no. 19; pp. 11253 - 11267
• Main Authors: Mhashal, Anil R, Romero-Rivera, Adrian, Mydy, Lisa S, Cristobal, Judith R, Gulick, Andrew M, Richard, John P, Kamerlin, Shina C. L
• Format: Journal Article
• Language: English
• Published: United States American Chemical Society 02.10.2020
• Subjects: empirical valence bond; glycerol-3-phosphate dehydrogenase; Hamiltonian replica exchange; loop dynamics; transition state stabilization; glycerol-3-phosphate dehydrogenase; Hamiltonian replica exchange; transition state stabilization; loop dynamics; empirical valence bond

Glycerol-3-phosphate dehydrogenase is a biomedically important enzyme that plays a crucial role in lipid biosynthesis. It is activated by a ligand-gated conformational change that is necessary for the enzyme to reach a catalytically competent conformation capable of efficient transition-state stabil...