Functional role of arginine residues in glutamic acid decarboxylase from brain and bacteria.
The arginine-specific reagent phenylglyoxal rapidly inactives glutamic decarboxylase from both mouse brain and E. coli when preincubated with the enzyme at concentrations of 3 mM to 40 mM. The rate of inactivation follows pseudo-first-order kinetics and is dependent upon the concentration of phenylglyoxal. These and other data presented support the idea that arginine residues play a key role in the mechanism of action of glutamic decarboxylase.
D000818:Animals; D001120:Arginine; D001921:Brain / Q000201:enzymology*; D002262:Carboxy-Lyases / Q000037:antagonists & inhibitors / Q000378:metabolism; D004926:Escherichia coli / Q000201:enzymology*; D005968:Glutamate Decarboxylase / Q000037:antagonists & inhibitors / Q000378:metabolism; D006037:Glyoxal / Q000031:analogs & derivatives / Q000494:pharmacology; D008297:Male; D051379:Mice
D006037:Glyoxal; D001120:Arginine; D002262:Carboxy-Lyases; D005968:Glutamate Decarboxylase