The βG156C substitution in the F1-ATPase from the thermophilic Bacillus PS3 affects catalytic site cooperativity by destabilizing the closed conformation of the catalytic site

Biochemistry

Volumn 41, Issue 48, 2002, Pages 14421-14429

  Bandyopadhyay, Sanjay ^a   Valder, Carolina R ^a   Huynh, Hue G ^a   Ren, Huimiao ^a   Allison, William S ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

MUTANTS;

ADENOSINETRIPHOSPHATE; CATALYSIS; CONFORMATIONS; FLUORESCENCE; HYDROLYSIS; STOICHIOMETRY; TITRATION;

BIOCHEMISTRY;

ADENOSINE TRIPHOSPHATASE; BACTERIAL ENZYME; CYTOSINE; GUANINE; TUNGSTEN; VANADIUM; YTTRIUM; ADENOSINE TRIPHOSPHATE; CYSTEINE; DIMETHYLAMINE; GLUTAMIC ACID; GLYCINE; MAGNESIUM; N,N DIMETHYLDODECYLAMINE OXIDE; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATASE; SODIUM AZIDE; TRYPTOPHAN; TYROSINE; VALINE;

AMINO ACID SUBSTITUTION; ARTICLE; BINDING AFFINITY; CATALYSIS; CHEMICAL MODIFICATION; COMPLEX FORMATION; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME ACTIVITY; FLUORESCENCE; HYDROLYSIS; NONHUMAN; PRIORITY JOURNAL; STOICHIOMETRY; THERMOPHILIC BACTERIUM; TURNOVER TIME; BACILLUS; BINDING SITE; CHEMISTRY; COMPARATIVE STUDY; ENZYME STABILITY; ENZYMOLOGY; GENETICS; METABOLISM; PROTEIN CONFORMATION; SITE DIRECTED MUTAGENESIS;

BACTERIA (MICROORGANISMS); INSERTION SEQUENCES;

ADENOSINE TRIPHOSPHATE; AMINO ACID SUBSTITUTION; BACILLUS; BINDING SITES; CATALYSIS; CATALYTIC DOMAIN; CYSTEINE; DIMETHYLAMINES; ENZYME STABILITY; GLUTAMIC ACID; GLYCINE; HYDROLYSIS; MAGNESIUM; MUTAGENESIS, SITE-DIRECTED; PROTEIN CONFORMATION; PROTON-TRANSLOCATING ATPASES; SODIUM AZIDE; TRYPTOPHAN; TYROSINE; VALINE;

EID: 0037015829     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi026243g     Document Type: Article

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