A single mutation at the catalytic site of TF1-α3β3γ complex switches the kinetics of ATP hydrolysis from negative to positive cooperativity

FEBS Letters

Volumn 413, Issue 1, 1997, Pages 55-59

  Muneyuki, Eiro ^a   Odaka, Masafumi ^b   Yoshida, Masasuke ^a  

^a TOKYO INSTITUTE OF TECHNOLOGY   (Japan)

^b INST OF PHYS AND CHEMICAL RESEARCH   (Japan)

Author keywords

Binding change model; Cooperative kinetics; F1 ATPase

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE;

ARTICLE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME KINETICS; MUTATION; PRIORITY JOURNAL; THERMOPHILIC BACTERIUM;

ADENOSINE TRIPHOSPHATE; ALANINE; BINDING SITES; CATALYSIS; CYSTEINE; DOSE-RESPONSE RELATIONSHIP, DRUG; HYDROLYSIS; KINETICS; LEUCINE; MATHEMATICS; MUTATION; PROTON-TRANSLOCATING ATPASES; TYROSINE;

BACTERIA (MICROORGANISMS);

EID: 0030796982     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0014-5793(97)00878-8     Document Type: Article

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