Role of Phe283 in enzymatic reaction of cyclodextrin glycosyltransferase from alkalophilic Bacillus sp.1011: Substrate binding and arrangement of the catalytic site

Protein Science

Volumn 13, Issue 2, 2004, Pages 457-465

  Kanai, Ryuta ^a,b   Haga, Keiko ^a   Akiba, Toshihiko ^b   Yamane, Kunio ^a   Harata, Kazuaki ^b  

^a UNIVERSITY OF TSUKUBA   (Japan)

^b NATIONAL INSTITUTE OF ADVANCED INDUSTRIAL SCIENCE AND TECHNOLOGY AIST   (Japan)

Author keywords

Catalytic activity; CGTase; Crystal structure; Substrate binding

Indexed keywords

ACARBOSE; AMYLASE; ASPARTIC ACID; CARBOXYL GROUP; CYCLOMALTODEXTRIN GLUCANOTRANSFERASE; HISTIDINE; HYDROXYL GROUP; LEUCINE; PHENYLALANINE; STARCH; TYROSINE;

ARTICLE; BACILLUS; CATALYSIS; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME BINDING; ENZYME MECHANISM; ENZYME STABILITY; ENZYME STRUCTURE; ENZYME SUBSTRATE; GENE MUTATION; GLYCOSYLATION; HYDROGEN BOND; NONHUMAN; PH; PRIORITY JOURNAL; PROTEIN FAMILY; TEMPERATURE DEPENDENCE; WILD TYPE;

ACARBOSE; BACILLUS; BINDING SITES; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; GLUCOSYLTRANSFERASES; HYDROGEN BONDING; HYDROGEN-ION CONCENTRATION; KINETICS; LYSINE; MODELS, MOLECULAR; MUTATION; PHENYLALANINE; PLIABILITY; PROTEIN STRUCTURE, TERTIARY; SUBSTRATE SPECIFICITY; TYROSINE;

BACILLUS SP.; BACILLUS SP. 1011;

EID: 1642452924     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.03408504     Document Type: Article

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