Escherichia coli contains a protein that is homologous in function and N-terminal sequence to the protein encoded by the nifS gene of Azotobacter vinelandii and that can participate in the synthesis of the Fe-S cluster of dihydroxy-acid dehydratase

Journal of Biological Chemistry

Volumn 271, Issue 27, 1996, Pages 16068-16074

  Flint, Dennis H ^a  

^a DUPONT COMPANY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CYSTEINE; DIHYDROXYACID DEHYDRATASE; IRON SULFUR PROTEIN; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ARTICLE; AZOTOBACTER VINELANDII; DISULFIDE BOND; ESCHERICHIA COLI; GENE CLUSTER; OXIDATION; PRIORITY JOURNAL; PROTEIN PURIFICATION; PROTEIN SYNTHESIS; SEQUENCE HOMOLOGY; STRUCTURE ACTIVITY RELATION;

ALANINE; AMINO ACID SEQUENCE; AZOTOBACTER VINELANDII; BACTERIAL PROTEINS; CHROMATOGRAPHY, GEL; CHROMATOGRAPHY, ION EXCHANGE; CYSTEINE; DISULFIDES; ESCHERICHIA COLI; GENES, BACTERIAL; HAEMOPHILUS INFLUENZAE; HYDRO-LYASES; IRON-SULFUR PROTEINS; KINETICS; MACROMOLECULAR SUBSTANCES; MOLECULAR SEQUENCE DATA; NAPHTHALENESULFONATES; PANTETHEINE; PEPTIDE FRAGMENTS; PYRIDOXAL PHOSPHATE; SEQUENCE HOMOLOGY, AMINO ACID; SULFHYDRYL REAGENTS;

AZOTOBACTER VINELANDII; BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 0030018746     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

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