Kinetic and structural consequences of replacing the aspartate bridge by asparagine in the catalytic metal triad of Escherichia coli alkaline phosphatase

Journal of Molecular Biology

Volumn 257, Issue 3, 1996, Pages 700-715

  Tibbitts, Thomas T ^a   Murphy, Jennifer E ^a   Kantrowitz, Evan R ^a  

^a BOSTON COLLEGE   (United States)

Author keywords

Carboxylate bridge; Magnesium activation; Metalloenzymes; Protein structure function; X ray crystallography

Indexed keywords

ALANINE; ALKALINE PHOSPHATASE; ASPARAGINE; ASPARTIC ACID; BACTERIAL ENZYME; MAGNESIUM ION; ZINC;

ARTICLE; ENZYME ACTIVITY; ENZYME KINETICS; ENZYME STRUCTURE; ENZYME SUBUNIT; ESCHERICHIA COLI; NONHUMAN; PH; PRIORITY JOURNAL; SITE DIRECTED MUTAGENESIS; X RAY CRYSTALLOGRAPHY;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; FELIS CATUS;

EID: 0029931998     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1996.0195     Document Type: Article

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