Active site and laminarin binding in glycoside hydrolase family 55

Journal of Biological Chemistry

Volumn 290, Issue 19, 2015, Pages 11819-11832

  Bianchetti, Christopher M ^a,b   Takasuka, Taichi E ^a,c   Deutsch, Sam ^d   Udell, Hannah S ^a   Yik, Eric J ^e   Bergeman, Lai F ^a   Fox, Brian G ^a  

^a UNIVERSITY OF WISCONSIN MADISON   (United States)

^b UNIVERSITY OF WISCONSIN OSHKOSH   (United States)

^c HOKKAIDO UNIVERSITY   (Japan)

^d DOE JOINT GENOME INSTITUTE   (United States)

^e CALIFORNIA STATE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AROMATIC COMPOUNDS; ENZYME ACTIVITY; ENZYMES; HYDROLASES; SUBSTRATES; SUGARS;

CONFORMATIONAL FLEXIBILITY; EXPERIMENTAL METHODS; FUNCTIONAL COVERAGE; FUNCTIONAL PROPERTIES; GLYCOSIDE HYDROLASES; HIGH RESOLUTION CRYSTAL STRUCTURE; HYDROLYSIS REACTION; PHANEROCHAETE CHRYSOSPORIUM;

CRYSTAL STRUCTURE;

GLUCAN SYNTHASE; GLUCOSE; GLUTAMINE; GLYCOSIDASE; LAMINARAN; LAMINARIHEXAOSE; LAMINARITETRAOSE; LAMINARITRIOSE; NUCLEOPHILE; POLYSACCHARIDE; SACTELAM55A PROTEIN; UNCLASSIFIED DRUG; WATER; BACTERIAL PROTEIN; GLUCAN; PROTEIN BINDING;

ARTICLE; CATALYSIS; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVATION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME BINDING; ENZYME CONFORMATION; ENZYME SUBSTRATE COMPLEX; GENE SYNTHESIS; MUTAGENESIS; PRIORITY JOURNAL; PROTEIN HYDROLYSIS; STREPTOMYCES; STRUCTURE ACTIVITY RELATION; BIOLOGY; CHEMICAL STRUCTURE; CHEMISTRY; ENZYMOLOGY; ESCHERICHIA COLI; HYDROLYSIS; METABOLISM; MUTATION; PH; PHANEROCHAETE; PHYLOGENY; X RAY CRYSTALLOGRAPHY;

BACTERIA (MICROORGANISMS); FUNGI; PHANEROCHAETE CHRYSOSPORIUM; STREPTOMYCES SP.;

BACTERIAL PROTEINS; CATALYSIS; CATALYTIC DOMAIN; COMPUTATIONAL BIOLOGY; CRYSTALLOGRAPHY, X-RAY; ESCHERICHIA COLI; GLUCANS; GLYCOSIDE HYDROLASES; HYDROGEN-ION CONCENTRATION; HYDROLYSIS; MODELS, MOLECULAR; MUTAGENESIS; MUTATION; PHANEROCHAETE; PHYLOGENY; POLYSACCHARIDES; PROTEIN BINDING; STREPTOMYCES; WATER;

EID: 84929095679     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.623579     Document Type: Article

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