Specificity of processing α-glucosidase I is guided by the substrate conformation: Crystallographic and in silico studies

Journal of Biological Chemistry

Volumn 288, Issue 19, 2013, Pages 13563-13574

  Barker, Megan K ^a   Rose, David R ^a,b  

^a PRINCESS MARGARET HOSPITAL   (Canada)

^b UNIVERSITY OF WATERLOO   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

GLUCOSIDASE; IN-SILICO;

BIOCHEMISTRY; BIOLOGY;

ENZYMES;

ALPHA GLUCOSIDASE; ALPHA GLUCOSIDASE 1; GLYCAN; N ACETYLGLUCOSAMINE; UNCLASSIFIED DRUG;

ARTICLE; COMPUTER MODEL; CRYSTALLOGRAPHY; ENZYME ACTIVE SITE; ENZYME BINDING; ENZYME CONFORMATION; ENZYME MECHANISM; ENZYME SPECIFICITY; ENZYME STRUCTURE; ENZYME SUBSTRATE; GENE MUTATION; GENETIC CONSERVATION; MOLECULAR DOCKING; PRIORITY JOURNAL; PROTEIN FOLDING;

CARBOHYDRATE GLYCOPROTEIN; COMPUTER MODELING; DOCKING; ENZYME STRUCTURE; GLYCOBIOLOGY; GLYCOSYLATION; POST-TRANSLATIONAL MODIFICATION; X-RAY CRYSTALLOGRAPHY;

1-DEOXYNOJIRIMYCIN; ALPHA-GLUCOSIDASES; CARBOHYDRATE CONFORMATION; CARBOHYDRATE SEQUENCE; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; GLUCOSE; HYDROGEN BONDING; KINETICS; MEMBRANE GLYCOPROTEINS; MOLECULAR DOCKING SIMULATION; MOLECULAR SEQUENCE DATA; PROTEIN BINDING; PROTEIN STRUCTURE, SECONDARY; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; STRUCTURAL HOMOLOGY, PROTEIN; SUBSTRATE SPECIFICITY; TRISACCHARIDES;

EID: 84877713668     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.460436     Document Type: Article

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