Structure of a complex of Thermoactinomyces vulgaris R-47 α-amylase 2 with maltohexaose demonstrates the important role of aromatic residues at the reducing end of the substrate binding cleft

Carbohydrate Research

Volumn 341, Issue 8, 2006, Pages 1041-1046

  Ohtaki, Akashi ^a   Mizuno, Masahiro ^a   Yoshida, Hiromi ^b   Tonozuka, Takashi ^a   Sakano, Yoshiyuki ^a   Kamitori, Shigehiro ^a,b  

^a TOKYO UNIVERSITY OF AGRICULTURE AND TECHNOLOGY   (Japan)

^b KAGAWA UNIVERSITY   (Japan)

Author keywords

Amylase; Enzymatic glucoside hydrolysis; Maltohexaose; X ray structure

Indexed keywords

AROMATIC COMPOUNDS; DIMERS; ENZYMES; OLIGOMERS; POLYSACCHARIDES; X RAY ANALYSIS;

Α-AMYLASE; ENZYMATIC GLUCOSIDE HYDROLYSIS; MALTOHEXAOSE; X-RAY STRUCTURE;

MOLECULAR STRUCTURE;

ALANINE; AMYLASE; CYCLODEXTRIN; ENZYME; MALTOSE; OLIGOSACCHARIDE; STARCH; TRYPTOPHAN; WATER;

ARTICLE; BINDING AFFINITY; CATALYSIS; CONFORMATION; CRYSTAL STRUCTURE; ENZYME STRUCTURE; HYDROGEN BOND; HYDROLYSIS; KINETICS; MOLECULAR INTERACTION; NONHUMAN; PRIORITY JOURNAL; STRUCTURE ANALYSIS; THERMOACTINOMYCES VULGARIS;

ALANINE; ALPHA-AMYLASE; AMINO ACID SUBSTITUTION; AMINO ACIDS, AROMATIC; BINDING SITES; CATALYSIS; CRYSTALLOGRAPHY, X-RAY; DIMERIZATION; HYDROGEN BONDING; HYDROLYSIS; KINETICS; MICROMONOSPORACEAE; MODELS, MOLECULAR; OLIGOSACCHARIDES; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SUBSTRATE SPECIFICITY; TRYPTOPHAN; TYROSINE; WATER;

THERMOACTINOMYCES VULGARIS;

EID: 33646158199     PISSN: 00086215     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.carres.2006.01.029     Document Type: Article

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