Interaction of chloride with yeast aminopeptidase I. Equilibrium binding studies.
The effect of chloride on metal binding by yeast aminopeptidase I, as well as the binding of chloride to various enzyme forms were studied by means of a micro-centrifugation technique using radioactive 36Cl- as a ligand. Chloride did not significantly alter the binding of activating Zn2+, or binding of Co2+ to the essential metal sites. Both the native Zn2+ enzyme and Co2+-substituted aminopeptidase I bind stoichiometric amounts of C1- (1 Cl-/subunit) with apparent dissociation constants of 0.1-0.2 mM. Additional Cl- was bound at higher concentrations. In contrast to the metal-containing enzyme forms the apoenzyme did not express the high-affinity chloride binding site.
D000626:Aminopeptidases / Q000378:metabolism*; D001665:Binding Sites; D002712:Chlorides / Q000378:metabolism* / Q000494:pharmacology; D003035:Cobalt / Q000378:metabolism; D007700:Kinetics; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D029701:Saccharomyces cerevisiae Proteins; D015032:Zinc / Q000378:metabolism
D002712:Chlorides; D029701:Saccharomyces cerevisiae Proteins; D003035:Cobalt; D000626:Aminopeptidases; C019689:APE1 protein, S cerevisiae; D015032:Zinc