L-Glutamate decarboxylase.
Much progress has been made in recent years regarding enzymological aspects of mammalian brain GAD, such as its purification and characterization, but some uncertainty still remains concerning its molecular weight and forms, and its subunit structure. The availability of antibodies to this enzyme has allowed immunocytochemical studies which have provided important information on the intrinsic organization of GABA-ergic neurones in the CNS, particularly in the cerebellum and nigrostriatal pathway. With the increased understanding of the enzymology of GAD and the distribution of central GABA-ergic neurones, it is becoming feasible to study the regulatory biochemistry of GAD in terms of control and adaptive mechanisms at the cellular level. In our own laboratory, as well as in others, initial approaches have already begun. Obviously, cellular regulation of this phenotypic enzyme is an important issue for the understanding of GABA-ergic neurones and their functions.
D000109:Acetylcholine / Q000494:pharmacology; D000469:Alkaline Phosphatase / Q000494:pharmacology; D000818:Animals; D001921:Brain / Q000201:enzymology*; D002262:Carboxy-Lyases / Q000378:metabolism*; D002525:Cerebellar Cortex / Q000187:drug effects / Q000201:enzymology; D004789:Enzyme Activation; D004926:Escherichia coli / Q000201:enzymology; D005968:Glutamate Decarboxylase / Q000378:metabolism*; D007700:Kinetics; D008970:Molecular Weight; D013116:Spinal Cord / Q000201:enzymology*; D014018:Tissue Distribution
D000469:Alkaline Phosphatase; D002262:Carboxy-Lyases; D005968:Glutamate Decarboxylase; D000109:Acetylcholine