Aromatic rings of tyrosine residues at adenine nucleotide binding sites of the beta subunits of F1-ATPase are not necessary for ATPase activity.
Using site-directed mutagenesis, Tyr-307, Tyr-341, or Tyr-364, supposedly located at the adenine nucleotide binding site(s) of the beta subunits of F1-ATPase from the thermophilic bacterium PS3, was replaced with Phe or Cys. The alpha 3 beta 3 complexes reconstituted from the alpha subunits and individual mutant beta subunits hydrolyzed ATP. Thus, neither the hydroxyl groups nor the aromatic rings in these positions are required for ATPase activity of F1-ATPase.
Odaka
M
M
Department of Life Science, Tokyo Institute of Technology, Yokohama, Japan.
Kobayashi
H
H
Muneyuki
E
E
Yoshida
M
M
D000255:Adenosine Triphosphate / Q000378:metabolism; D001483:Base Sequence; D001665:Binding Sites; D004252:DNA Mutational Analysis; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics; D007700:Kinetics; D046911:Macromolecular Substances; D008969:Molecular Sequence Data; D009711:Nucleotides / Q000378:metabolism; D006180:Proton-Translocating ATPases / Q000235:genetics / Q000378:metabolism*; D013329:Structure-Activity Relationship; D014443:Tyrosine
D046911:Macromolecular Substances; D009711:Nucleotides; D014443:Tyrosine; D000255:Adenosine Triphosphate; D006180:Proton-Translocating ATPases