Structural and biochemical characterization of glycoside hydrolase family 79 β-glucuronidase from Acidobacterium capsulatum

Journal of Biological Chemistry

Volumn 287, Issue 17, 2012, Pages 14069-14077

  Michikawa, Mari ^a   Ichinose, Hitomi ^a   Momma, Mitsuru ^b   Biely, Peter ^c   Jongkees, Seino ^d   Yoshida, Makoto ^e   Kotake, Toshihisa ^f   Tsumuraya, Yoichi ^f   Withers, Stephen G ^d   Fujimoto, Zui ^b   Kaneko, Satoshi ^a  

^a FOOD RESEARCH INSTITUTE   (Japan)

^b NATIONAL INSTITUTE OF AGROBIOLOGICAL SCIENCES   (Japan)

^c INSTITUTE OF CHEMISTRY   (Slovakia)

^d UNIVERSITY OF BRITISH COLUMBIA   (Canada)

^e TOKYO UNIVERSITY OF AGRICULTURE AND TECHNOLOGY   (Japan)

^f SAITAMA UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

ACID BASE; BIOCHEMICAL CHARACTERIZATION; CARBOXYL GROUPS; CATALYTIC RESIDUE; D-GLUCURONIC ACID; EQUIVALENT PARAMETERS; GLUCOSIDASE; GLUCOSIDASE ACTIVITY; GLUCURONIDASE; GLYCOSIDE HYDROLASES; MAIN CHAINS; NMR ANALYSIS; O-METHYL GROUP; PRODUCT COMPLEX; SUBSTRATE DISCRIMINATION; TRACE LEVEL; WILD TYPES; WILD-TYPE ENZYMES; WILD-TYPE LEVELS; XYLOSIDASE;

ENZYMES; FUNCTIONAL GROUPS; GLUCOSE;

PLANTS (BOTANY);

79 BETA GLUCURONIDASE; ALANINE; BETA GLUCURONIDASE; GLUCURONIC ACID; GLUTAMIC ACID; GLUTAMINE; GLYCINE; TYROSINE; UNCLASSIFIED DRUG; XYLAN 1,4 BETA XYLOSIDASE;

ACIDOBACTERIUM CAPSULATUM; ARTICLE; BINDING SITE; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME MECHANISM; ENZYME SUBSTRATE; LIGAND BINDING; MUTATIONAL ANALYSIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN MOTIF; PROTEIN PROTEIN INTERACTION; PROTON NUCLEAR MAGNETIC RESONANCE; RESIDUE ANALYSIS; STRUCTURE ACTIVITY RELATION; STRUCTURE ANALYSIS;

ACIDOBACTERIA; BINDING SITES; CATALYSIS; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; GLUCURONIDASE; GLYCOSIDE HYDROLASES; KINETICS; MODELS, MOLECULAR; MUTAGENESIS; MUTATION; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; SUBSTRATE SPECIFICITY;

EID: 84859958875     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.346288     Document Type: Article

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