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Volumn 271, Issue 17, 1996, Pages 10109-10115
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Mutation of Tyr235 in the NAD (H)-binding subunit of the proton-translocating nicotinamide nucleotide transhydrogenase of Rhodospirillum rubrum affects the conformational dynamics of a mobile loop and lowers the catalytic activity of the enzyme
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Author keywords
[No Author keywords available]
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Indexed keywords
ESCHERICHIA COLI;
RHODOSPIRILLUM RUBRUM;
ASPARAGINE;
BACTERIAL ENZYME;
MUTANT PROTEIN;
NICOTINAMIDE ADENINE DINUCLEOTIDE (PHOSPHATE) TRANSHYDROGENASE;
PHENYLALANINE;
RECOMBINANT PROTEIN;
REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE;
TYROSINE;
DRUG DERIVATIVE;
NICOTINAMIDE ADENINE DINUCLEOTIDE;
TRYPTOPHAN;
AMINO ACID SUBSTITUTION;
ARTICLE;
ELECTRON TRANSPORT;
ENZYME ACTIVITY;
ENZYME CONFORMATION;
ENZYME MECHANISM;
ENZYME SUBUNIT;
NONHUMAN;
PRIORITY JOURNAL;
PROTEIN DOMAIN;
PROTEIN PURIFICATION;
PROTON TRANSPORT;
RHODOSPIRILLUM RUBRUM;
BINDING SITE;
CATALYSIS;
CHEMISTRY;
ENZYMOLOGY;
METABOLISM;
NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY;
PROTEIN CONFORMATION;
SPECTROFLUOROMETRY;
STRUCTURE ACTIVITY RELATION;
TRANSPORT AT THE CELLULAR LEVEL;
ASPARAGINE;
BINDING SITES;
BIOLOGICAL TRANSPORT;
CATALYSIS;
MAGNETIC RESONANCE SPECTROSCOPY;
NAD;
NADP TRANSHYDROGENASE;
PHENYLALANINE;
PROTEIN CONFORMATION;
RHODOSPIRILLUM RUBRUM;
SPECTROMETRY, FLUORESCENCE;
STRUCTURE-ACTIVITY RELATIONSHIP;
TRYPTOPHAN;
TYROSINE;
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EID: 0029664405
PISSN: 00219258
EISSN: None
Source Type: Journal
DOI: 10.1074/jbc.271.17.10109 Document Type: Article |
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Times cited : (17)
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References (22)
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