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Article

A single mutation at the catalytic site of TF1-alpha3beta3gamma complex switches the kinetics of ATP hydrolysis from negative to positive cooperativity.

FEBS letters - 11 Aug 1997

Muneyuki E, Odaka M, Yoshida M

Abstract excerpt

Previously, we reported the substitution of Tyr341 of the F1-ATPase beta subunit from a thermophilic Bacillus strain PS3 with leucine, cysteine, or alanine (M. Odaka et al. J. Biochem., 115 (1994) 789-796). These mutations resulted in a great decrease in the affinity of the isolated beta subunit...

Topics

Adenosine Triphosphate
Alanine
Binding Sites
Catalysis
Cysteine
Dose-Response Relationship, Drug
Hydrolysis
Kinetics
Leucine
Mathematics
Mutation
Proton-Translocating ATPases

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Tyrosine

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Identifiers

PMID: 9287116
DOI: 10.1016/s0014-5793(97)00878-8

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-9287116-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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A single mutation at the catalytic site of TF1-alpha3beta3gamma complex switches the kinetics of ATP hydrolysis from negative to positive cooperativity.PMID 9287116Read ↗

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