Interaction of Human 3-Phosphoglycerate Kinase with Its Two Substrates: Is Substrate Antagonism a Kinetic Advantage?

• Published in: Journal of molecular biology Vol. 409; no. 5; pp. 742 - 757
• Main Authors: Lallemand, Perrine, Chaloin, Laurent, Roy, Béatrice, Barman, Tom, Bowler, Matthew W., Lionne, Corinne
• Format: Journal Article
• Language: English
• Published: England Elsevier Ltd 24.06.2011; Elsevier
• Subjects: adenosine diphosphate; adenosine triphosphate; Chemical Sciences; crystallographic structure; dissociation; enzyme kinetics; enzyme substrates; Humans; Kinetics; metabolism; Organic chemistry; phosphoglycerate kinase; Phosphoglycerate Kinase - metabolism; rapid-quench-flow; stopped-flow; Substrate Specificity; transient kinetics; transition-state analogue; stopped-flow; rapid-quench-flow; transient kinetics; PGK; crystallographic structure; transition-state analogue; PG; bPG; hPGK; PDB; Transient kinetics

Substrate antagonism has been described for a variety of enzymes with more than one substrate and is characterized by a lowering of the affinity of one substrate in the presence of the other(s). 3-Phosphoglycerate kinase (PGK) catalyzes phosphotransfer from 1,3-bisphosphoglycerate (bPG) to ADP to gi...