FAD is a preferred substrate and an inhibitor of Escherichia coli general NAD(P)H:flavin oxidoreductase

Journal of Biological Chemistry

Volumn 277, Issue 42, 2002, Pages 39450-39455

  Louie, Tai Man ^a   Yang, Haw ^b   Karnchanaphanurach, Pallop ^c   Sunney Xie, X ^d   Xun, Luying ^a  

^a WASHINGTON STATE UNIVERSITY   (United States)

^b HARVARD UNIVERSITY   (United States)

^c Kemin Industries Inc   (United States)

^d UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; COMPUTER SIMULATION; CONFORMATIONS; ESCHERICHIA COLI; HYDROGEN BONDS; SUBSTRATES;

ELECTRON ACCEPTOR;

BIOCHEMISTRY;

ADENOSINE DIPHOSPHATE; ADENOSINE PHOSPHATE; FLAVINE ADENINE NUCLEOTIDE; FLAVINE MONONUCLEOTIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE DEHYDROGENASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE FLAVIN OXIDOREDUCTASE; RIBOFLAVIN; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; BINDING AFFINITY; BINDING SITE; COMPETITIVE INHIBITION; COMPLEX FORMATION; COMPUTER SIMULATION; CONCENTRATION RESPONSE; ELECTRON TRANSPORT; ENZYME ACTIVITY; ENZYME CONFORMATION; ENZYME INHIBITION; ENZYME REPRESSION; ENZYME SUBSTRATE COMPLEX; ESCHERICHIA COLI; HYDROGEN BOND; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; REACTION ANALYSIS; REDUCTION; STRUCTURE ANALYSIS;

BINDING SITES; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; DOSE-RESPONSE RELATIONSHIP, DRUG; ELECTRONS; ENZYME INHIBITORS; ESCHERICHIA COLI; FLAVIN-ADENINE DINUCLEOTIDE; FMN REDUCTASE; HYDROGEN; KINETICS; MASS SPECTROMETRY; MODELS, CHEMICAL; PROTEIN BINDING; PROTEIN CONFORMATION; SPECTROMETRY, FLUORESCENCE; TIME FACTORS;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; NEGIBACTERIA;

EID: 0037131229     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M206339200     Document Type: Article

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