Two nucleophilic mutants of the Micromonospora viridifaciens sialidase operate with retention of configuration by two different mechanisms

ChemBioChem

Volumn 6, Issue 11, 2005, Pages 1999-2004

  Watson, Jacqueline N ^a   Newstead, Simon ^b,c   Narine, Arun A ^a   Taylor, Garry ^b   Bennet, Andrew J ^a  

^a SIMON FRASER UNIVERSITY   (Canada)

^b UNIVERSITY OF ST ANDREWS   (United Kingdom)

^c IMPERIAL COLLEGE LONDON   (United Kingdom)

Author keywords

Enzyme catalysis; Mutagenesis; Neuraminidase; Sialic acids; Sialidase

Indexed keywords

BACTERIAL ENZYME; GLUTAMINE; SIALIDASE;

ADDITION REACTION; ARTICLE; CATALYST; CELL MUTANT; CRYSTAL STRUCTURE; DISSOCIATION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME MECHANISM; ENZYME STRUCTURE; MICROMONOSPORA; MICROMONOSPORA VIRIDIFACIENS; PHASE TRANSITION; PRIORITY JOURNAL; STRUCTURE ANALYSIS;

AMINO ACID SUBSTITUTION; BINDING SITES; CRYSTALLOGRAPHY, X-RAY; KINETICS; MICROMONOSPORA; MOLECULAR STRUCTURE; MUTAGENESIS; NEURAMINIDASE; PROTEIN CONFORMATION; WATER;

BACTERIA (MICROORGANISMS); MICROMONOSPORA; MICROMONOSPORA VIRIDIFACIENS;

EID: 27744503583     PISSN: 14394227     EISSN: None     Source Type: Journal    
DOI: 10.1002/cbic.200500114     Document Type: Article

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