Structure and energetics of the glucoamylase-isomaltose transition-state complex probed by using modeling and deoxygenated substrates coupled with site-directed mutagenesis

Journal of Molecular Biology

Volumn 263, Issue 1, 1996, Pages 79-89

  Frandsen, Torben P ^a   Stoffer, Bjarne B ^a,c   Palcic, Monica M ^b   Hof, Suzanne ^b   Svensson, Birte ^a  

^a CARLSBERG LABORATORY   (Denmark)

^b UNIVERSITY OF ALBERTA   (Canada)

^c UNIVERSITY OF COPENHAGEN   (Denmark)

Author keywords

Active site mutants; Methyl isomaltoside and methyl 6 R C methyl isomaltoside analogs; Modeled glucoamylase isomaltose (trans gauche) complex; Substrate binding subsites; Substrate key polar groups

Indexed keywords

GLUCAN 1,4 ALPHA GLUCOSIDASE; ISOMALTOSE;

AMINO ACID SUBSTITUTION; ARTICLE; ASPERGILLUS NIGER; CATALYSIS; ENERGY TRANSFER; ENZYME CONFORMATION; ENZYME KINETICS; ENZYME SUBSTRATE; HYDROGEN BOND; HYDROLYSIS; MOLECULAR MODEL; NONHUMAN; PRIORITY JOURNAL; SITE DIRECTED MUTAGENESIS; STEREOCHEMISTRY; STRUCTURE ACTIVITY RELATION;

ASPERGILLUS NIGER; FELIS CATUS;

EID: 0030592505     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1996.0557     Document Type: Article

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