Crystal structures of the starch-binding domain from Rhizopus oryzae glucoamylase reveal a polysaccharide-binding path

Biochemical Journal

Volumn 416, Issue 1, 2008, Pages 27-36

  Tung, Jung Yu ^a   Chang, Margaret Dah Tsyr ^a   Chou, Wei I ^a   Liu, Yen Yi ^a   Yeh, Yi Hung ^a   Chang, Fan Yu ^a   Lin, Shu Chuan ^a   Qiu, Zhen Liang ^a   Sun, Yuh Ju ^a  

^a NATIONAL TSING HUA UNIVERSITY   (Taiwan)

Author keywords

cyclodextrin; Carbohydrate binding module; Maltohepataose; Rhizopus oryzae glucoamylase; Starch binding domain

Indexed keywords

ASPARAGINE RESIDUE; CARBOHYDRATE BINDING; CARBOHYDRATE-BINDING MODULE; CATALYTIC DOMAINS; CONFORMATIONAL CHANGE; D-GLUCOSE; FUNCTIONAL DOMAINS; GLUCOAMYLASE; GLYCOSYLATED; HYDROPHOBIC INTERACTIONS; MALTOHEPATAOSE; MALTOHEPTAOSE; N-TERMINAL; QUANTITATIVE BINDING; RHIZOPUS ORYZAE; RHIZOPUS ORYZAE GLUCOAMYLASE; SCATCHARD ANALYSIS; STARCH-BINDING DOMAIN; SUGAR BINDING;

BINDING ENERGY; BIOPOLYMERS; CARBOHYDRATES; ENZYMES; GLUCOSE; HYDROPHOBICITY; POLYSACCHARIDES; STARCH; SUGAR (SUCROSE);

BINDING SITES;

ASPARAGINE; BETA CYCLODEXTRIN; GLUCAN 1,4 ALPHA GLUCOSIDASE; HEPTOSE; MALTOSE; STARCH; TRYPTOPHAN; TYROSINE; BETA CYCLODEXTRIN DERIVATIVE;

AMINO TERMINAL SEQUENCE; ARTICLE; BINDING KINETICS; CARBOXY TERMINAL SEQUENCE; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; ENZYME STRUCTURE; FUNGAL GENETICS; HYDROPHOBICITY; ISOTHERM; MOLECULAR INTERACTION; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; QUANTITATIVE ANALYSIS; RHIZOPUS ORYZAE; SCATCHARD PLOT; X RAY DIFFRACTION; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; BINDING SITE; CHEMICAL STRUCTURE; CHEMISTRY; CRYSTALLIZATION; ENZYMOLOGY; GENETICS; METABOLISM; MOLECULAR GENETICS; PROTEIN TERTIARY STRUCTURE; RHIZOPUS; SEQUENCE ALIGNMENT; X RAY CRYSTALLOGRAPHY;

RHIZOPUS ORYZAE;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; BETA-CYCLODEXTRINS; BINDING SITES; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; GLUCAN 1,4-ALPHA-GLUCOSIDASE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN STRUCTURE, TERTIARY; RHIZOPUS; SEQUENCE ALIGNMENT; STARCH;

EID: 56049109995     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20080580     Document Type: Article

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