Escherichia coli methionine aminopeptidase: Implications of crystallographic analyses of the native, mutant, and inhibited enzymes for the mechanism of catalysis

Biochemistry

Volumn 38, Issue 24, 1999, Pages 7678-7688

  Lowther, W Todd ^a   Orville, Allen M ^a   Madden, David T ^a   Lim, Sejin ^b   Rich, Daniel H ^b   Matthews, Brian W ^a  

^a UNIVERSITY OF OREGON   (United States)

^b UNIVERSITY OF WISCONSIN MADISON   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; AMINO ACID; AMINOPEPTIDASE; COBALT; ENZYME INHIBITOR; HISTIDINE; HYDROXIDE; HYDROXYL GROUP; METHIONINE; MONOVALENT CATION; MUTANT PROTEIN; NITROGEN; SOLVENT;

AMINO ACID SUBSTITUTION; AMINO TERMINAL SEQUENCE; ARTICLE; BINDING SITE; CATALYSIS; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME INHIBITION; ESCHERICHIA COLI; LIGATION; NONHUMAN; PRIORITY JOURNAL; X RAY CRYSTALLOGRAPHY;

AMINOPEPTIDASES; BINDING SITES; CATALYSIS; CATIONS, MONOVALENT; COBALT; CRYSTALLOGRAPHY, X-RAY; ENZYME INHIBITORS; ESCHERICHIA COLI; HISTIDINE; HOLOENZYMES; LEUCINE; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; OLIGOPEPTIDES; ZINC;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 0033564306     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi990684r     Document Type: Article

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