title: Effect of conformation of the substrate on enzymatic decarboxylation of alpha-arylmalonic acid.
abstract: 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.
authors.affiliation: Department of Chemistry, Keio University, Yokohama, Japan.
authors.forename: K
authors.initials: K
authors.lastname: Miyamoto
authors.forename: H
authors.initials: H
authors.lastname: Ohta
authors.forename: Y
authors.initials: Y
authors.lastname: Osamura
mesh_terms: 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
chemical_list: D008314:Malonates; D002262:Carboxy-Lyases; C071852:malonate decarboxylase