Hydrogen exchange/electrospray ionization mass spectrometry studies of substrate and inhibitor binding and conformational changes of Escherichia coli dihydrodipicolinate reductase

Biochemistry

Volumn 36, Issue 13, 1997, Pages 3755-3759

  Wang, Fang ^a   Blanchard, John S ^a   Tang, Xue Jun ^a,b  

^a ALBERT EINSTEIN COLLEGE OF MEDICINE   (United States)

^b PFIZER INC   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; DEUTERIUM; DIPICOLINIC ACID; HYDROGEN; LYSINE; OXIDOREDUCTASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE;

AMINO ACID SYNTHESIS; ARTICLE; CONFORMATIONAL TRANSITION; ENZYME CONFORMATION; ENZYME SUBSTRATE; ESCHERICHIA COLI; ION EXCHANGE; MASS SPECTROMETRY; PRIORITY JOURNAL; PROTEIN DOMAIN;

AMINO ACID SEQUENCE; CHROMATOGRAPHY, LIQUID; DEUTERIUM; DIHYDRODIPICOLINATE REDUCTASE; ENZYME INHIBITORS; ESCHERICHIA COLI; HYDROGEN; MASS SPECTROMETRY; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; NAD; OXIDOREDUCTASES; OXIDOREDUCTASES ACTING ON CH-CH GROUP DONORS; PEPSIN A; PEPTIDE FRAGMENTS; PICOLINIC ACIDS; PROTEIN BINDING; PROTEIN CONFORMATION;

EID: 0030992108     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi963065g     Document Type: Article

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