Essential arginines in mercuric reductase isolated from Yersinia enterocolitica 138A14.
The mercuric reductase from Yersinia enterocolitica 138A14 was inactivated by the arginine modifying reagents 2,3-butanedione and phenylglyoxal. The inactivation by 2,3-butanedione exhibited second order kinetics with rate constant of 32 min-1 M-1. In the case of phenylglyoxal, biphasic kinetics were observed. The oxidized coenzyme (NADP+) prevented inactivation of the enzyme by the alpha-dicarbonyl reagents, whereas the reduced coenzyme (NADPH) enhanced the inactivation rate. The loss of enzyme activity was related to the incorporation of [2-14C] phenylglyoxal; when two arginines per subunit were modified the enzyme was completely inactivated.
Blaghen
M
M
Laboratoire de Biochimie, Faculté des Sciences I Université Hassan II, Casablanca, Morocco.
el Kebbaj
M S
MS
Vidon
D J
DJ
Tritsch
D
D
D001120:Arginine / Q000031:analogs & derivatives / Q000737:chemistry*; D001665:Binding Sites; D003931:Diacetyl / Q000494:pharmacology; D004789:Enzyme Activation; D004795:Enzyme Stability / Q000187:drug effects; D007700:Kinetics; D009249:NADP / Q000378:metabolism; D010088:Oxidoreductases / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000302:isolation & purification*; D010658:Phenylglyoxal / Q000494:pharmacology; D015008:Yersinia enterocolitica / Q000737:chemistry / Q000201:enzymology*
D009249:NADP; D001120:Arginine; D010088:Oxidoreductases; C021551:mercuric reductase; D003931:Diacetyl; D010658:Phenylglyoxal