Abstract:
:Crayfish glutamic acid decarboxylase (GAD), like the homologous enzymes from other species, is inhibited by carbonyl-trapping agents (e.g. aminooxyacetic acid; AOAA) and sulfhydryl reagents (e.g. 5,5'-dithiobis-(2-nitrobenzoic acid); DTNB). It also is inhibited by the product GABA, many anions (e.g. SCN- and Cl-), and some cations (e.g. Zn+2). The inhibition by AOAA, but not that by DTNB, was prevented by increasing the concentration of the pyridoxal phosphate (PLP) coenzyme. GABA blocked the effects of PLP on enzyme activity. The inhibition by AOAA, DTNB, GABA, and chloride all were competitive with substrate. The effect of GABA occurs at physiological concentrations and may contribute to the regulation of GAD activity in vivo. The quantitative effect of anions is dependent on the cation with which they are administered. ATP stimulated GAD activity in homogenates prepared with potassium phosphate or Tris-acetate buffer, even when no exogenous PLP was provided.
journal_name
Neurochem Resjournal_title
Neurochemical researchauthors
Grossfeld RM,Yancey SW,Baxter CFdoi
10.1007/BF00964526subject
Has Abstractpub_date
1984-07-01 00:00:00pages
947-63issue
7eissn
0364-3190issn
1573-6903journal_volume
9pub_type
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