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Literature summary for 7.1.2.2 extracted from

  • Bandyopadhyay, S.; Muneyuki, E.; Allison, W.S.
    The characteristics of the (alpha V371C)3(beta R337C)3 gamma double mutant subcomplex of the TF1-ATPase indicate that the catalytic site at the alpha TP-beta TP interface with bound MgADP in crystal structures of MF1 represents a catalytic site containing (2005), Biochemistry, 44, 2441-2448.
    View publication on PubMed

Application

Application Comment Organism
additional information the catalytic site at the alphaTP-betaTP interface is loaded first upon addition of nucleotides to nucleotide-depleted F1-ATPases Escherichia coli

Cloned(Commentary)

Cloned (Comment) Organism
mutant plasmids expressed in Escherichia coli strain JM103 Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
catalytic site at the alphaTP-betaTP interface with bound MgADP- in crystal structures represents a catalytic site containing inhibitory MgADP- Escherichia coli

Protein Variants

Protein Variants Comment Organism
additional information (alpha V371C)3(beta R337C)3 gamma double mutant, steady state ATPase activity is 30% of that of the wild-type Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
AlCl3 irreversibly inactivates the steady state ATPase activity of the reduced double mutant or the cross-linked enzyme after incubation of stoichiometric or 0.2 mM MgADP- Escherichia coli
MgADP- irreversibly inactivates the steady state ATPase activity of the reduced double mutant or the cross-linked enzyme after addition of AlCl3 and NaF Escherichia coli
NaF irreversibly inactivates the steady state ATPase activity of the reduced double mutant or the cross-linked enzyme after incubation of stoichiometric or 0.2 mM MgADP- Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
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-
-

Synonyms

Synonyms Comment Organism
TF1-ATPase
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Escherichia coli