Stereochemistry of reactions catalyzed by glutamate decarboxylase.
When the decarboxylation of L-glutamic acid by the glutamate decarboxylase from Escherichia coli is carried out in D2O, the product gamma-aminobutyric acid contains a single deuterium atom. The stereochemistry of this material was established by conversion to levorotatory methyl 4-phthalimido [4(-2)H] butyrate. The dextrorotatory isomer of the latter compound was synthesized from S-[2(-2)H] glycine by a series of reactions not affecting the stereochemistry at the chiral center. Thus, the decarboxylation of glutamic acid occurs with retention of configuration. Decarboxylation of L-alpha-methylglutamic acid by this enzyme produced levorotatory gamma-aminovaleric acid and thus also occurs with retention of configuration.
D000613:Aminobutyrates; D002262:Carboxy-Lyases / Q000378:metabolism*; D003903:Deuterium; D004926:Escherichia coli / Q000201:enzymology; D005968:Glutamate Decarboxylase / Q000378:metabolism*; D008968:Molecular Conformation; D009904:Optical Rotation; D013237:Stereoisomerism
D000613:Aminobutyrates; D003903:Deuterium; D002262:Carboxy-Lyases; D005968:Glutamate Decarboxylase