Studies on the synthesis of the Fe-S cluster of dihydroxy-acid dehydratase in Escherichia coli crude extract: Isolation of O-acetylserine sulfhydrylases A and B and β-cystathionase based on their ability to mobilize sulfur from cysteine and to participate in Fe-S cluster synthesis

Journal of Biological Chemistry

Volumn 271, Issue 27, 1996, Pages 16053-16067

  Flint, Dennis H ^a   Tuminello, Joseph F ^a   Miller, Thomas J ^a  

^a DUPONT COMPANY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; CYSTEINE SYNTHASE; DIHYDROXYACID DEHYDRATASE; DITHIOTHREITOL; IRON SULFUR PROTEIN; UNCLASSIFIED DRUG;

ARTICLE; CONTROLLED STUDY; ENZYME ISOLATION; ENZYME MECHANISM; ENZYME PURIFICATION; ENZYME STRUCTURE; ENZYME SYNTHESIS; ESCHERICHIA COLI; GENE CLUSTER; PRIORITY JOURNAL; PROTEIN METABOLISM;

AMINO ACID SEQUENCE; APOENZYMES; CHROMATOGRAPHY, GEL; CHROMATOGRAPHY, ION EXCHANGE; CYSTEINE; CYSTEINE SYNTHASE; ESCHERICHIA COLI; HYDRO-LYASES; IRON; IRON-SULFUR PROTEINS; ISOENZYMES; KINETICS; LYASES; MOLECULAR SEQUENCE DATA; MOLECULAR WEIGHT; RADIOISOTOPE DILUTION TECHNIQUE; SEQUENCE HOMOLOGY, AMINO ACID; SPECTROPHOTOMETRY; SUBSTRATE SPECIFICITY; SULFUR RADIOISOTOPES;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; PUFFINUS AURICULARIS;

EID: 0030056113     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.271.27.16053     Document Type: Article

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