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Literature summary for 7.1.2.2 extracted from

  • Loebau, S.; Weber, J.; Senior, A.E.
    Nucleotide occupancy of F1-ATPase catalytic sites under crystallization conditions (1997), FEBS Lett., 404, 15-18.
    View publication on PubMed
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Crystallization (Commentary)

Crystallization (Comment) Organism
site-directed tryptophan fluorescence technique can provide valuable support for F1 crystallography studies Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Reaction

Reaction Comment Organism Reaction ID
ATP + H2O + 4 H+[side 1] = ADP + phosphate + 4 H+[side 2] X-ray structure is compatible with a catalytic mechanism in which all three F1-ATPase catalytic sites must fill with MgATP to initiate steady-state hydrolysis Escherichia coli
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + H+/in
-
 Escherichia coli ADP + phosphate + H+/out
-
 ?