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Journal of Biological Chemistry

Volumn 277, Issue 1, 2002, Pages 50-58

Escherichia coli γ-glutamylcysteine synthetase. Two active site metal ions affect substrate and inhibitor binding

(3) Kelly, Brenda S a,b Antholine, William E a,b Griffith, Owen W a,b

a Department of Biochemistry ^* (United States)

b MEDICAL COLLEGE OF WISCONSIN (United States)

Author keywords

[No Author keywords available]

Indexed keywords

MAMMALIAN ISOFORMS;

AMINO ACIDS; BIOSYNTHESIS; CATALYSIS;

ESCHERICHIA COLI;

BUTHIONINE SULFOXIMINE; COPPER ION; GLUTAMATE CYSTEINE LIGASE; LIGAND; MAGNESIUM ION; MANGANESE; METAL ION;

ARTICLE; BINDING AFFINITY; BIOSYNTHESIS; CATALYSIS; CONTROLLED STUDY; ELECTRON SPIN RESONANCE; ENZYME ACTIVE SITE; ENZYME ASSAY; ENZYME BINDING; ENZYME INACTIVATION; ENZYME MECHANISM; ENZYME SPECIFICITY; ENZYME SUBSTRATE; ESCHERICHIA COLI; NONHUMAN; PEPTIDE SYNTHESIS; PRIORITY JOURNAL;

BINDING SITES; BUTHIONINE SULFOXIMINE; COPPER; ELECTRON SPIN RESONANCE SPECTROSCOPY; ESCHERICHIA COLI; GLUTAMATE-CYSTEINE LIGASE; HUMANS; MAGNESIUM; MANGANESE;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; EUKARYOTA; MAMMALIA; NEGIBACTERIA; PROKARYOTA;

EID: 0037016697 PISSN: 00219258 EISSN: None Source Type: Journal
DOI: 10.1074/jbc.M107961200 Document Type: Article

Times cited : (52)

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