Crystal structure of an inverting GH 43 1,5-α-L-arabinanase from Geobacillus stearothermophilus complexed with its substrate

Biochemical Journal

Volumn 422, Issue 1, 2009, Pages 73-82

  Alhassid, Anat ^a   Ben David, Alon ^b   Tabachnikov, Orly ^b   Libster, Dima ^a   Naveh, Einat ^b   Zolotnitsky, Gennady ^b   Shoham, Yuval ^b   Shoham, Gil ^a  

^a HEBREW UNIVERSITY OF JERUSALEM   (Israel)

^b TECHNION ISRAEL INSTITUTE OF TECHNOLOGY   (Israel)

Author keywords

Arabinanase; Catalytic mechanism; Crystal structure; Enzyme substrate complex; Glycoside hydrolase; Substrate specificity

Indexed keywords

ARABINANASE; CATALYTIC MECHANISM; ENZYME-SUBSTRATE COMPLEX; GLYCOSIDE HYDROLASE; SUBSTRATE SPECIFICITY;

AMINO ACIDS; CARBOXYLATION; COBALT COMPOUNDS; ENZYMES; HYDROGEN; HYDROGEN BONDS; HYDROLYSIS; MOLECULES; POLYSACCHARIDES; SUBSTRATES; SUGARS;

CRYSTAL STRUCTURE;

1,5 ALPHA LEVO ARABINANASE; ARABINAN; ARABINOBIOSE; ARABINOSE; ARABINOSE DERIVATIVE; ARABINOTRIOSE; ASPARTIC ACID; CARBOXYLIC ACID; GLUTAMIC ACID; GLYCOSIDASE; POLYSACCHARIDE; UNCLASSIFIED DRUG;

ARTICLE; BIOCHEMISTRY; CATALYSIS; CONTROLLED STUDY; CRYSTAL STRUCTURE; CRYSTALLIZATION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME PURIFICATION; ENZYME SPECIFICITY; ENZYME SUBSTRATE COMPLEX; GEOBACILLUS STEAROTHERMOPHILUS; HYDROGEN BOND; IMAGE QUALITY; ISOTHERMAL TITRATION CALORIMETRY; MOLECULAR CLONING; MOLECULAR RECOGNITION; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN HYDROLYSIS; PROTEIN LOCALIZATION; REDUCTION; STRUCTURAL HOMOLOGY; STRUCTURE ANALYSIS; VISCOSITY;

BACILLUS STEAROTHERMOPHILUS; BIOCATALYSIS; CATALYTIC DOMAIN; CLONING, MOLECULAR; CRYSTALLOGRAPHY, X-RAY; GLYCOSIDE HYDROLASES; SUBSTRATE SPECIFICITY; THERMODYNAMICS;

GEOBACILLUS STEAROTHERMOPHILUS;

EID: 68749112865     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20090180     Document Type: Article

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