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Characterization and function of catalytic subunit a of H/sup +/-translocating adenosine triphosphatase from vacuolar membranes of Saccharomyces cerevisiae

Journal Article · · J. Biol. Chem.; (United States)
OSTI ID:7075858

Subunit a (M/sub r/ 89,000) from vacuolar membrane H/sup +/-translocating adenosine triphosphatase of the yeast Saccharomyces cerevisiae was found to bind 8-azido(..cap alpha..-/sup 32/P)adenosine triphosphate. Labeling by this photosensitive ATP derivative was saturable with an apparent dissociation constant of 10/sup -6/ to 10/sup -5/ M and decreased in the presence of ATP and ADP. The enzyme was inactivated by 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole (NBD-Cl), with about 1 ..mu..M causing half-maximal inactivation in the neutral pH range. This inactivation was prevented by the presence of ATP, ADP, or adenosyl-5'-yl imidodiphosphate (AMP-PNP). The original activity was restored by treating the inactivated enzyme with 2-mercaptoethanol. Kinetic and chemical studies of the inactivation showed that the activity was lost on chemical modification of a single tyrosine residue per molecule of the enzyme. When the enzyme was inactivated with (/sup 14/C)NBD-Cl, subunit a was specifically labeled, and this labeling was completely prevented by the presence of ATP, GTP, ADP, or AMP-PNP. From these results, it was concluded that subunit a of yeast vacuolar H/sup +/-ATPase has a catalytic site that contains a single, essential tyrosine residue. The kinetics of single site hydrolysis of (..gamma..-/sup 32/P)ATP indicated the formation of an enzyme-ATP complex and subsequent hydrolysis of bound ATP to ADP and P/sub i/ at the NBD-Cl-sensitive catalytic site.

Research Organization:
Univ. of Tokyo (Japan)
OSTI ID:
7075858
Journal Information:
J. Biol. Chem.; (United States), Journal Name: J. Biol. Chem.; (United States) Vol. 263:1; ISSN JBCHA
Country of Publication:
United States
Language:
English