The family 21 carbohydrate-binding module of glucoamylase from Rhizopus oryzae consists of two sites playing distinct roles in ligand binding

Biochemical Journal

Volumn 396, Issue 3, 2006, Pages 469-477

  Chou, Wei I ^a   Pai, Tun Wen ^b   Liu, Shi Hwei ^a   Hsiung, Bor Kai ^a   Chang, Margaret D T ^a  

^a NATIONAL TSING HUA UNIVERSITY   (Taiwan)

^b NATIONAL TAIWAN OCEAN UNIVERSITY   (Taiwan)

Author keywords

Binding affinity; Carbohydrate binding module (CBM); Glucoamylase (GA); Homology modelling; Progressive secondary structure correlation (PSSC); Starch binding domain (SBD)

Indexed keywords

CARBOHYDRATES; CATALYSIS; HYDROLYSIS; MOLECULAR STRUCTURE; MUTAGENESIS; POLYSACCHARIDES; SPECTROSCOPIC ANALYSIS; STARCH;

BINDING AFFINITY; CARBOHYDRATE-BINDING MODULE (CBM); GLUCOAMYLASE (GA); HOMOLOGY MODELING; PROGRESSIVE SECONDARY STRUCTURE CORRELATION (PSSC); STARCH-BINDING DOMAIN (SBD);

ENZYMES;

CARBOHYDRATE; CARBOHYDRATE BINDING PROTEIN; GLUCAN 1,4 ALPHA GLUCOSIDASE; POLYSACCHARIDE; TRYPTOPHAN; TYROSINE; CYCLODEXTRIN; LIGAND; N BROMOSUCCINIMIDE; OLIGOSACCHARIDE; STARCH; TETRANITROMETHANE;

ARTICLE; BINDING AFFINITY; DATA ANALYSIS; LIGAND BINDING; MOLECULAR MODEL; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN PURIFICATION; PROTEIN SECONDARY STRUCTURE; RHIZOPUS ORYZAE; SITE DIRECTED MUTAGENESIS; SPECTROSCOPY; AMINO ACID SEQUENCE; BINDING SITE; CHEMICAL STRUCTURE; CHEMISTRY; CIRCULAR DICHROISM; ENZYMOLOGY; GENETICS; METABOLISM; MOLECULAR GENETICS; PHYSIOLOGY; PROTEIN TERTIARY STRUCTURE; RHIZOPUS; SEQUENCE ALIGNMENT; ULTRAVIOLET SPECTROPHOTOMETRY;

RHIZOPUS ORYZAE;

AMINO ACID SEQUENCE; BINDING SITES; BROMOSUCCINIMIDE; CIRCULAR DICHROISM; CYCLODEXTRINS; GLUCAN 1,4-ALPHA-GLUCOSIDASE; LIGANDS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; OLIGOSACCHARIDES; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; RHIZOPUS; SEQUENCE ALIGNMENT; SPECTROPHOTOMETRY, ULTRAVIOLET; STARCH; TETRANITROMETHANE; TRYPTOPHAN; TYROSINE;

EID: 33744986320     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20051982     Document Type: Article

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