Effect of conformation of the substrate on enzymatic decarboxylation of alpha-arylmalonic acid.
The configuration and conformation of a compound are critical factors that determine whether it can be accepted by an enzyme as a substrate or not. We have examined enzyme-catalyzed decarboxylation of some alpha-substituted malonic acids and proposed that the syn-periplanar conformation is required for the substrates to be bound to the active site of the enzyme. Theoretical calculation of potential energy surfaces also supports the conclusion from experimental results.
Miyamoto
K
K
Department of Chemistry, Keio University, Yokohama, Japan.
Ohta
H
H
Osamura
Y
Y
D000421:Alcaligenes / Q000201:enzymology; D002262:Carboxy-Lyases / Q000378:metabolism*; D009682:Magnetic Resonance Spectroscopy; D008314:Malonates / Q000737:chemistry* / Q000378:metabolism; D008958:Models, Molecular; D008968:Molecular Conformation; D011048:Polarography; D013379:Substrate Specificity; D013816:Thermodynamics
D008314:Malonates; D002262:Carboxy-Lyases; C071852:malonate decarboxylase