The noncatalytic triad of α-amylases: A novel structural motif involved in conformational stability

Proteins: Structure, Function and Genetics

Volumn 70, Issue 2, 2008, Pages 320-328

  Marx, Jean Claude ^a   Poncin, Johan ^a   Simorre, Jean Pierre ^b   Ramteke, Pramod W ^c   Feller, Georges ^a,d  

^a UNIVERSITY OF LIÈGE   (Belgium)

^b INSTITUT DE BIOLOGIE STRUCTURALE   (France)

^c SAM HIGGINBOTTOM UNIVERSITY OF AGRICULTURE   (India)

^d Institute of Chemistry B6a   (Belgium)

Author keywords

amylase; Catalytic triad; Low barrier hydrogen bond; Protease; Protein stability

Indexed keywords

AMYLASE; CHLORIDE; GLUTAMIC ACID; GLYCOSIDE; HISTIDINE; HYDROLASE; MUTANT PROTEIN; PROTEIN SH2; PROTON; SERINE;

ARTICLE; CATALYSIS; ENZYME ACTIVATION; ENZYME ACTIVE SITE; ENZYME CONFORMATION; HYDROGEN BOND; NITROGEN NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN MOTIF; PROTEIN STABILITY; PROTON NUCLEAR MAGNETIC RESONANCE;

ALPHA-AMYLASE; CATALYSIS; ENZYME STABILITY; MUTAGENESIS, SITE-DIRECTED; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN CONFORMATION; PSEUDOALTEROMONAS;

BACTERIA (MICROORGANISMS);

EID: 37849041615     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.21594     Document Type: Article

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