Inactivation of enolase from carp (Cyprinus carpio) muscle by 2,3-butanedione.
Enolase from white muscle of carp (Cyprinus carpio) is inactivated by 2,3-butanedione in borate buffer. Magnesium ions as well as substrate--2-phosphoglycerate markedly altered the rate and extent of inactivation. The partially inactivated enzyme shows unaltered Km but decreased Vmax after 10 min incubation with butanedione, however after 60 min incubation the Km value increased 2.5 fold.
Pietkiewicz
J
J
Department of Biochemistry, Medical School, Wrocław, Poland.
Wolny
M
M
D000818:Animals; D001881:Borates; D002021:Buffers; D002347:Carps; D003931:Diacetyl / Q000494:pharmacology*; D004586:Electrophoresis; D005988:Glyceric Acids / Q000494:pharmacology; D007700:Kinetics; D008274:Magnesium / Q000494:pharmacology; D009132:Muscles / Q000201:enzymology*; D010751:Phosphopyruvate Hydratase / Q000037:antagonists & inhibitors* / Q000737:chemistry
D001881:Borates; D002021:Buffers; D005988:Glyceric Acids; C008885:2-phosphoglycerate; D010751:Phosphopyruvate Hydratase; D008274:Magnesium; D003931:Diacetyl