Protein motions promote catalysis.
A relationship between molecular dynamics motions of noncatalytic residues and enzyme activity has recently been proposed. We present examples where mutations either near or distal from the active site residues modify internal enzyme motion with resulting modification of catalysis. A better understanding of internal protein motions correlated to catalysis will lead to a greater insight into enzyme function.
Département de Chimie, Université de Montréal, Montréal, Québec, H3C 3J7, Canada.
Audrey
A
Tousignant
Joelle N
JN
Pelletier
D000818:Animals; D002384:Catalysis; D008099:Liver / Q000201:enzymology; D009038:Motion; D010088:Oxidoreductases / Q000737:chemistry / Q000378:metabolism*; D014305:Triose-Phosphate Isomerase / Q000737:chemistry / Q000378:metabolism*; D001618:beta-Lactamases / Q000737:chemistry / Q000378:metabolism*
D010088:Oxidoreductases; D001618:beta-Lactamases; D014305:Triose-Phosphate Isomerase