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Literature summary extracted from

  • Chen, W.; Hu, C.Y.; Crampton, D.J.; Frasch, W.D.
    Characterization of the metal binding environment of catalytic site 1 of chloroplast F1-ATPase from Chlamydomonas (2000), Biochemistry, 39, 9393-9400.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
7.1.2.2 D262C modification of beta-subunit, mutation causes large changes in the 51V hyperfine tensor of VO2+-nucleotide bound to site 1 Chlamydomonas reinhardtii
7.1.2.2 D262H modification of beta-subunit, mutation causes large changes in the 51V hyperfine tensor of VO2+-nucleotide bound to site 1 Chlamydomonas reinhardtii
7.1.2.2 D262T modification of beta-subunit, mutation causes large changes in the 51V hyperfine tensor of VO2+-nucleotide bound to site 1 Chlamydomonas reinhardtii
7.1.2.2 E197C modification of beta-subunit, mutation impairs ATP synthase and ATPase activity catalyzed by CF1F0 and soluble CF1 respectively. Mutation causes large changes in the 51V hyperfine tensor of VO2+-nucleotide bound to site 1 but not to site 3 Chlamydomonas reinhardtii
7.1.2.2 E197D modification of beta-subunit, mutation impairs ATP synthase and ATPase activity catalyzed by CF1F0 and soluble CF1 respectively. Mutation causes large changes in the 51V hyperfine tensor of VO2+-nucleotide bound to site 1 but not to site 3 Chlamydomonas reinhardtii
7.1.2.2 E197S modification of beta-subunit, mutation impairs ATP synthase and ATPase activity catalyzed by CF1F0 and soluble CF1 respectively. Mutation causes large changes in the 51V hyperfine tensor of VO2+-nucleotide bound to site 1 but not to site 3 Chlamydomonas reinhardtii

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining

Organism

EC Number Organism UniProt Comment Textmining
7.1.2.2 Chlamydomonas reinhardtii
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-
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
7.1.2.2 ATP + H2O + H+/in
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 Chlamydomonas reinhardtii ADP + phosphate + H+/out
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 ?