Divalent metal activation of a GH43 β-xylosidase

Enzyme and Microbial Technology

Volumn 52, Issue 2, 2013, Pages 84-90

  Lee, Charles C ^a   Braker, Jay D ^b   Grigorescu, Arabela A ^c   Wagschal, Kurt ^a   Jordan, Douglas B ^b  

^a WESTERN REGIONAL RESEARCH CENTER   (United States)

^b NATIONAL CENTER FOR AGRICULTURAL UTILIZATION RESEARCH   (United States)

^c NORTHWESTERN UNIVERSITY   (United States)

Author keywords

Xylosidase; Divalent cation; Hemicellulose; Multimerization

Indexed keywords

ACTIVE SITE; CATALYTIC MECHANISMS; CHEMICAL FEEDSTOCKS; D-GLUCOSE; DIVALENT CATION; DIVALENT METAL CATIONS; DIVALENT METALS; GLYCOSIDE HYDROLASES; HEMICELLULOSE; LIGNOCELLULOSIC BIOMASS; MIXED MICROBIAL CULTURE; MULTIMERIZATION; POTENTIAL SITES; SEDIMENTATION EQUILIBRIUM; SIDE-CHAINS; TEMPERATURE STABILITY; TRANSPORTATION FUELS; XYLOBIOSES; XYLOSIDASE;

AMINO ACIDS; CENTRIFUGATION; CLONING; ENZYMES; GENE ENCODING; GLUCOSE; MANGANESE; MANGANESE COMPOUNDS; POSITIVE IONS; SACCHARIFICATION;

METALS;

4 NITROPHENYL ALPHA LEVO ARABINOFURANOSIDE; 4 NITROPHENYL LEVO DEXTRO XYLOPYRANOSIDE; AMINO ACID; ARABINOBIOSE; ARABINOSE DERIVATIVE; CALCIUM; CARBOHYDRATE DERIVATIVE; CATION; COBALT; COPPER; DIMER; GLUCOSE; GLYCOSIDASE; GLYCOSIDASE 43; IRON; MAGNESIUM; MANGANESE; METAL; NICKEL; TETRAMER; UNCLASSIFIED DRUG; XYLAN; XYLAN 1,4 BETA XYLOSIDASE; XYLOBIOSE; ZINC;

ARTICLE; CARBOXYLATION; CATALYSIS; CENTRIFUGATION; ENZYME ACTIVATION; ENZYME REACTOR; ENZYME STABILITY; ENZYME STRUCTURE; GENETIC CODE; METAL BINDING; MOLECULAR CLONING; NONHUMAN; PH MEASUREMENT; PROTEIN MULTIMERIZATION; SACCHARIFICATION; SEDIMENTATION RATE; TEMPERATURE;

AMINO ACID SEQUENCE; ANAEROBIOSIS; CATALYSIS; CATALYTIC DOMAIN; CATIONS, DIVALENT; CLONING, MOLECULAR; DNA; ENZYME ACTIVATION; ENZYME STABILITY; GENE LIBRARY; HYDROGEN-ION CONCENTRATION; KINETICS; MOLECULAR SEQUENCE DATA; PROTEIN STRUCTURE, QUATERNARY; RECOMBINANT FUSION PROTEINS; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID; SEWAGE; SUBSTRATE SPECIFICITY; TEMPERATURE; XYLOSIDASES;

EID: 84871704129     PISSN: 01410229     EISSN: 18790909     Source Type: Journal    
DOI: 10.1016/j.enzmictec.2012.10.010     Document Type: Article

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