Properties of gamma-glutamyl arylamidase activity of the heavy subunit of gamma-glutamyl arylamidase from Bacillus sp. strain No. 12.
gamma-Glutamyl arylamidase of Bacillus sp. strain No. 12, composed of two heavy (Mr 56,000) and two light (Mr 46,000) subunits, was dissociated and inactivated by mild SDS treatment. The activity was restored in the isolated heavy subunit but not in the light subunit when SDS was removed by dialysis. The restored activity of the heavy subunit was similar to that of the native enzyme with regard to substrate specificity and inhibition and activation by alpha- and gamma-glutamyl compounds, free amino acids, peptides, enzyme inhibitors, and anti-native enzyme antibody.
D000581:Amidohydrolases / Q000276:immunology / Q000302:isolation & purification*; D000596:Amino Acids / Q000494:pharmacology; D000906:Antibodies / Q000494:pharmacology; D001407:Bacillus / Q000201:enzymology*; D003956:Dialysis; D004789:Enzyme Activation; D005973:Glutamine / Q000494:pharmacology; D005978:Glutathione / Q000494:pharmacology; D006868:Hydrolysis; D007700:Kinetics; D010455:Peptides / Q000494:pharmacology; D013379:Substrate Specificity
D000596:Amino Acids; D000906:Antibodies; D010455:Peptides; D005973:Glutamine; D000581:Amidohydrolases; C047188:gamma-glutamylarylamidase; D005978:Glutathione