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Volumn 343, Issue 1, 1999, Pages 135-138
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α3β3γ complex of F1-ATPase from thermophilic Bacillus PS3 can maintain steady-state ATP hydrolysis activity depending on the number of non-catalytic sites
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Author keywords
ADP inhibition; F1 ATPase; Hybrid complex
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Indexed keywords
ADENOSINE TRIPHOSPHATASE (MAGNESIUM);
ADENOSINE TRIPHOSPHATE;
PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE;
DIMETHYLAMINE;
ENZYME ACTIVATOR;
N,N DIMETHYLDODECYLAMINE OXIDE;
PRIMER DNA;
PROTON TRANSPORTING ADENOSINE TRIPHOSPHATASE;
ARTICLE;
CATALYSIS;
COMPLEX FORMATION;
CONTROLLED STUDY;
ENZYME ACTIVE SITE;
ENZYME ACTIVITY;
ENZYME INACTIVATION;
ENZYME INHIBITION;
ENZYME ISOLATION;
HYDROLYSIS;
NONHUMAN;
PRIORITY JOURNAL;
THERMOPHILIC BACTERIUM;
BACILLUS;
ENZYMOLOGY;
GENETICS;
METABOLISM;
NUCLEOTIDE SEQUENCE;
SITE DIRECTED MUTAGENESIS;
ADENOSINE TRIPHOSPHATE;
BACILLUS;
BASE SEQUENCE;
CATALYTIC DOMAIN;
DIMETHYLAMINES;
DNA PRIMERS;
ENZYME ACTIVATORS;
HYDROLYSIS;
MUTAGENESIS, SITE-DIRECTED;
PROTON-TRANSLOCATING ATPASES;
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EID: 0033215273
PISSN: 02646021
EISSN: None
Source Type: Journal
DOI: 10.1042/0264-6021:3430135 Document Type: Article |
Times cited : (18)
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References (24)
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