Structural advantage of sugar beet α-glucosidase to stabilize the Michaelis complex with long-chain substrate

Journal of Biological Chemistry

Volumn 290, Issue 3, 2015, Pages 1796-1803

  Tagami, Takayoshi ^a,b   Yamashita, Keitaro ^a   Okuyama, Masayuki ^a   Mori, Haruhide ^a   Yao, Min ^a   Kimura, Atsuo ^a  

^a HOKKAIDO UNIVERSITY   (Japan)

^b RAKUNO GAKUEN UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

CHAINS; CRYSTAL STRUCTURE; CYCLODEXTRINS; ENZYME ACTIVITY; ENZYMES; STARCH; SUGAR BEETS; VAN DER WAALS FORCES;

HELICAL CONFORMATION; MALTOOLIGOSACCHARIDES; STEADY-STATE KINETICS; STRUCTURAL ADVANTAGE; STRUCTURAL FEATURE; STRUCTURAL INSIGHTS; SUBSTRATE SPECIFICITY; VAN DER WAALS INTERACTIONS;

SUBSTRATES;

ACARVIOSYL MALTOOLIGOSACCHARIDE; ALPHA GLUCOSIDASE; AMYLOSE; OLIGOSACCHARIDE; UNCLASSIFIED DRUG; CARBOHYDRATE; GLUCOSE; MALTOHEXAOSE; PROTEIN BINDING;

ARTICLE; CHEMICAL REACTION; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME BINDING; ENZYME CONFORMATION; ENZYME SPECIFICITY; ENZYME STABILITY; ENZYME SUBSTRATE; ENZYME SUBSTRATE COMPLEX; HYDROLYSIS; MICHAELIS MENTEN KINETICS; NONHUMAN; PROTEIN CARBOHYDRATE INTERACTION; REACTION ANALYSIS; STEADY STATE; STRUCTURE ACTIVITY RELATION; STRUCTURE ANALYSIS; SUGAR BEET; VAN DER WAALS INTERACTION; BEET; CHEMISTRY; CRYSTALLIZATION; ENZYMOLOGY; MOLECULAR GENETICS; NUCLEOTIDE SEQUENCE; SITE DIRECTED MUTAGENESIS;

BETA VULGARIS SUBSP. VULGARIS;

ALPHA-GLUCOSIDASES; BASE SEQUENCE; BETA VULGARIS; CARBOHYDRATES; CATALYTIC DOMAIN; CRYSTALLIZATION; GLUCOSE; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; OLIGOSACCHARIDES; PROTEIN BINDING; SUBSTRATE SPECIFICITY;

EID: 84922230719     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.606939     Document Type: Article

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