Catalysis by arginine deiminase: Evidence for a covalent intermediate

Autor: Douglas W. Smith, David E. Fahrney
Rok vydání: 1978
Předmět:
Zdroj: Biochemical and Biophysical Research Communications. 83:101-106
ISSN: 0006-291X
DOI: 10.1016/0006-291x(78)90403-5
Popis: Arginine deiminase (EC 3.5.3.6) catalyzes the hydrolysis of arginine to ammonia and citrulline. This reaction is postulated to occur in three steps: (1) formation of the Michaelis complex, (2) the formation of an amidino-enzyme intermediate and liberation of ammonia, and (3) the rate-determining step, hydrolysis of the amidino-enzyme. The enzymic reaction is accelerated 5-fold by 0.2 M imidazole. This striking effect is expected for the amidino-enzyme mechanism but otherwise is difficult to explain. The putative amidino-enzyme intermediate can be demonstrated by quenching the [14C]arginine-arginine deiminase reaction at low pH. Under these conditions, 0.5 equivalents of 14C label per mol enzyme dimer were covalently bound.
Databáze: OpenAIRE