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Volumn 271, Issue 27, 1996, Pages 16068-16074
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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
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Author keywords
[No Author keywords available]
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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;
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EID: 0030018746
PISSN: 00219258
EISSN: None
Source Type: Journal
DOI: None Document Type: Article |
Times cited : (190)
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References (20)
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