An hypothesis that each subtype of glutamate receptors requires a specific conformation of L-glutamate for its selective activation was examined using the conformationally constrained analogs of L-glutamate, L-2-(2-carboxycyclopropyl)glycines (CCGs), and L-2-[2-carboxy-3-(methoxymethyl)cyclopropyl)glycines (MCGs). All MCG isomers were newly synthesized in a stereoselective manner via the common synthetic intermediate 5a starting with the oxazolidine aldehyde 1. The synthesis of the four MCG isomers was characterized by a stereoselective inversion of alpha-cyclopropyl acyl anion (e.g., from 10 to 11). The spectroscopic studies, in particular, pH vs J correlation experiments of CCGs and MCGs using 1H NMR and their molecular mechanics calculations, revealed that these analogs possessed an antiperiplanar conformation regarding the H-C2-C1'-H bond as a majority among the other possible rotamers in aqueous solution. The fact that each CCG and MCG exhibited potent and selective activities to the distinct types of glutamate receptors allowed us to extract an active conformation of L-glutamate. Thus, the conformational requirement of metabotropic glutamate receptors was speculated to be the anti-anti conformation (aa-A) because the conformations of CCG-1 and cis and trans-MCG-I, selective agonists of the receptors, closely mimicked the rotamer A of L-glutamate. On the other hand, N-methyl-D-aspartate and kainate receptors, representative ionotropic glutamate receptors, would require glutamate g+g+ rotamer E which was deduced from the conformation-activity relationship studies of the selective agonists CCG-IV, cis-MCG-IV, and trans-MCG-IV and the related analogs.