Mutations at Glu-32 and His-39 in the epsilon subunit of the Escherichia coli F1F0 ATP synthase affect its inhibitory properties.
A collection of amino acid substitutions at residues Glu-32 and His-39 in the epsilon subunit of the Escherichia coli F1F0 ATP synthase has been constructed by cassette mutagenesis. Substitutions for residue Glu-32 appeared to cause abnormal inhibition of membrane-bound F1 ATPase activity, and replacement of His-39 by Arg, Val, and Pro affected F1F0 interactions.
Department of Biological Sciences, Southern Methodist University, Dallas, Texas 75275-0376.
D J
DJ
LaRoe
S B
SB
Vik
D000595:Amino Acid Sequence; D001483:Base Sequence; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics*; D005971:Glutamates / Q000235:genetics*; D018698:Glutamic Acid; D006639:Histidine / Q000235:genetics*; D008969:Molecular Sequence Data; D016254:Mutagenesis, Insertional; D010957:Plasmids; D006180:Proton-Translocating ATPases / Q000235:genetics* / Q000378:metabolism
D005971:Glutamates; D018698:Glutamic Acid; D006639:Histidine; D006180:Proton-Translocating ATPases