Probing impact of active site residue mutations on stability and activity of Neisseria polysaccharea amylosucrase

Protein Science

Volumn 22, Issue 12, 2013, Pages 1754-1765

  Daudé, David ^a,b,c   Topham, Christopher M ^a,b,c   Remaud Siméon, Magali ^a,b,c   André, Isabelle ^a,b,c  

^a UNIVERSITÉ DE TOULOUSE   (France)

^b CNRS   (France)

^c UMR792 INGÉNIERIE DES SYSTÈMES BIOLOGIQUES ET DES PROCÉDÉS   (France)

Author keywords

Amylosucrase; DSF; Enzyme engineering; Enzyme thermostability; GH 13 family; Structurebased approach

Indexed keywords

AMYLOSUCRASE; BACTERIAL ENZYME; GLYCOSIDASE; MUTANT PROTEIN; OLIGOSACCHARIDE; UNCLASSIFIED DRUG;

ALGORITHM; AMINO ACID SEQUENCE; ARTICLE; BIOCATALYST; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME ENGINEERING; ENZYME PURIFICATION; ENZYME STABILITY; ENZYME STRUCTURE; ENZYME SUBSTRATE; HIGH THROUGHPUT SCREENING; MELTING POINT; MUTATION; NEISSERIA; NEISSERIA POLYSACCHAREA; NONHUMAN; PRIORITY JOURNAL; SITE DIRECTED MUTAGENESIS; WILD TYPE;

AMYLOSUCRASE; DSF; ENZYME ENGINEERING; ENZYME THERMOSTABILITY; GH 13 FAMILY; STRUCTURE-BASED APPROACH;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; CATALYTIC DOMAIN; ENZYME STABILITY; EVOLUTION, MOLECULAR; GENETIC VARIATION; GLUCANS; GLUCOSYLTRANSFERASES; HYDROGEN BONDING; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; NEISSERIA; SUBSTRATE SPECIFICITY; THERMODYNAMICS;

EID: 84891636252     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.2375     Document Type: Article

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