Purification and characterization of wild-type and mutant 'classical' nitroreductases of Salmonella typhimurium. L33R mutation greatly diminishes binding of FMN to the nitroreductase of S. typhimurium

Journal of Biological Chemistry

Volumn 273, Issue 37, 1998, Pages 23922-23928

  Watanabe, Masahiko ^a,c   Nishino, Tatsuya ^a,d   Takio, Koji ^b   Sofuni, Toshio ^a   Nohmi, Takehiko ^a  

^a NATIONAL INSTITUTE OF HEALTH SCIENCES   (Japan)

^b INST OF PHYS AND CHEMICAL RESEARCH   (Japan)

^c NATIONAL CANCER CENTER RESEARCH INSTITUTE   (Japan)

^d BIOMOL ENG RESEARCH INSTITUTE   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE; BACTERIAL ENZYME; DNA; FLAVIN OXIDOREDUCTASE; FLAVINE MONONUCLEOTIDE; FLAVOPROTEIN; LEUCINE; NITROREDUCTASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE; UNCLASSIFIED DRUG;

ARTICLE; CONTROLLED STUDY; DNA SEQUENCE; ENTEROBACTER CLOACAE; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME PURIFICATION; ENZYME SPECIFICITY; ESCHERICHIA COLI; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; SALMONELLA TYPHIMURIUM; THERMUS THERMOPHILUS; VIBRIO;

AMINO ACID SEQUENCE; BASE SEQUENCE; BINDING SITES; CHROMATOGRAPHY; CHROMATOGRAPHY, GEL; CHROMATOGRAPHY, ION EXCHANGE; CLONING, MOLECULAR; DURAPATITE; ENTEROBACTER CLOACAE; ESCHERICHIA COLI; FLAVIN MONONUCLEOTIDE; HAEMOPHILUS; KINETICS; MOLECULAR SEQUENCE DATA; MOLECULAR WEIGHT; MYCOPLASMA; NITROREDUCTASES; POINT MUTATION; SALMONELLA TYPHIMURIUM; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID; THERMUS THERMOPHILUS; VIBRIO;

EID: 0032508631     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.273.37.23922     Document Type: Article

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