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Three catalytic sites in mitochondrial ATPase
Author(s) -
Cerdán E.,
Campo M.L.,
López-Moratalla N.,
Santiago E.
Publication year - 1983
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(83)80697-8
Subject(s) - atpase , chemistry , catalysis , substrate (aquarium) , enzyme , bicarbonate , biochemistry , binding site , atp hydrolysis , hydrolysis , mitochondrion , stereochemistry , biology , organic chemistry , ecology
Kinetic data obtained after determining the hydrolytic activity of ATPase from rat liver in preparations where the enzyme had been purified, or in mitochondria, strongly suggest the existence of three different catalytic sites with different affinity for the substrate. The results obtained when measuring the ATPase activity at different substrate concentrations, and in the presence of the inhibitors KOCN or KSCN, or of the activators dinitrophenol and bicarbonate, show that the binding of these compounds to a regulatory site or sites affects in a different degree the hydrolytic activity of each catalytic site.