Replacement of serine 373 by phenylalanine in the alpha subunit of Escherichia coli F1-ATPase results in loss of steady-state catalysis by the enzyme.

This publication has 47 references indexed in Scilit:

• Identification of the initially NBD-labeled essential tyrosine residue in bovine heart MF1-ATPase
  Biochemical and Biophysical Research Communications, 1983
• The proton-ATPase of bacteria and mitochondria
  The Journal of Membrane Biology, 1983
• A simple method for displaying the hydropathic character of a protein
  Journal of Molecular Biology, 1982
• Nucleotide sequence of the genes for β and ε subunits of proton-translocating ATPase from Escherichia coli
  Biochemical and Biophysical Research Communications, 1982
• Nucleotide sequence of the genes for F0 components of the proton-translocating ATPase from : Prediction of the primary structure of F0 subunits
  Biochemical and Biophysical Research Communications, 1981
• Nucleotide sequence of the gene coding for the δ subunit of proton-translocating ATPase of Escherichia coli
  Biochemical and Biophysical Research Communications, 1981
• Nucleotide sequence of genes coding for dicyclohexylcarbodiimide-binding protein and the α subunit of proton-translocating ATPase of Escherichia coli
  Biochemical and Biophysical Research Communications, 1981
• The uncA401 mutation alters a nucleotide-binding site in the α-subunit of the F₁ adenosine triphosphatase from Escherichia coli
  FEBS Letters, 1980
• Identfication of the altered subunit in the inactive F1ATPase of an Escherichia coli uncA mutant
  Biochemical and Biophysical Research Communications, 1978
• Reconstitution of ATPase activity from the isolated α, β, and γ subunits of the coupling factor, F1, of Escherichia coli
  Biochemical and Biophysical Research Communications, 1977