Substrate recognition by three family 13 yeast α-glucosidases: Evaluation of deoxygenated and conformationally biased isomaltosides

European Journal of Biochemistry

Volumn 269, Issue 2, 2002, Pages 728-734

  Frandsen, Torben P ^a,c   Palcic, Monica M ^b   Svensson, Birte ^a  

^a CARLSBERG LABORATORY   (Denmark)

^b UNIVERSITY OF ALBERTA   (Canada)

^c Santaris Pharma AS   (Denmark)

Author keywords

Glycosidase mechanism; Molecular recognition; NMR; Protein carbohydrate interaction; Substrate analogs

Indexed keywords

ALPHA GLUCOSIDASE; CARBOHYDRATE DERIVATIVE; FUNGAL ENZYME; GLUCAN 1,4 ALPHA GLUCOSIDASE; HYDROXYL GROUP; METHYL 6 S ETHYL ALPHA ISOMALTOSIDE; METHYL ALPHA ISOMALTOSIDE; OLIGO 1,6 GLUCOSIDASE; UNCLASSIFIED DRUG;

ARTICLE; ASPERGILLUS NIGER; CALCULATION; ELECTRICITY; ENERGY TRANSFER; ENZYME SPECIFICITY; ENZYME SUBSTRATE; HYDROGEN BOND; HYDROLYSIS; ISOMER; KINETICS; MOLECULAR RECOGNITION; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; OXYGENATION; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN FAMILY; STEREOCHEMISTRY; STRUCTURE ACTIVITY RELATION; STRUCTURE ANALYSIS; YEAST;

ALPHA-GLUCOSIDASES; CATALYSIS; HYDROLYSIS; MAGNETIC RESONANCE SPECTROSCOPY; SACCHAROMYCES CEREVISIAE; STEREOISOMERISM; SUBSTRATE SPECIFICITY;

ASPERGILLUS; ASPERGILLUS NIGER;

EID: 0036159556     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.0014-2956.2001.02714.x     Document Type: Article

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