Functional roles of H98 and W99 and β2α2 loop dynamics in the α- L -arabinofuranosidase from Thermobacillus xylanilyticus

FEBS Journal

Volumn 279, Issue 19, 2012, Pages 3598-3611

  Arab Jaziri, Faten ^a,b,c   Bissaro, Bastien ^a,b   Barbe, Sophie ^a,b   Saurel, Olivier ^a,d   Débat, Hélène ^e   Dumon, Claire ^a,b   Gervais, Virginie ^a,d   Milon, Alain ^a,e   André, Isabelle ^a,b   Fauré, Régis ^a,b   O'Donohue, Michael J ^a,b  

^a INSA   (France)

^b UMR792 INGÉNIERIE DES SYSTÈMES BIOLOGIQUES ET DES PROCÉDÉS   (France)

^c Agence de l'Environnement et de la Maëtrise de l'Energie   (France)

^d INSTITUT DE PHARMACOLOGIE ET DE BIOLOGIE STRUCTURALE   (France)

^e LABORATOIRE DES SCIENCES DU CLIMAT ET DE L ENVIRONNEMENT   (France)

Author keywords

l arabinofuranosidase; loop; glycoside hydrolase; molecular dynamics; STD NMR

Indexed keywords

4 NITROPHENYL ALPHA ARABINOFURANOSIDE; ALANINE; ALPHA ARABINOFURANOSIDASE; CHROMOGENIC SUBSTRATE; PHENYLALANINE; SOLVENT; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; CATALYSIS; ENTROPY; ENZYME ACTIVE SITE; ENZYME ANALYSIS; ENZYME KINETICS; ENZYME STRUCTURE; ENZYME SUBSTRATE COMPLEX; HYDROGEN BOND; ISOTHERMAL TITRATION CALORIMETRY; MOLECULAR DYNAMICS; MOLECULAR INTERACTION; MOLECULAR STABILITY; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN MOTIF; SATURATION TRANSFER DIFFERENCE NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; SITE DIRECTED MUTAGENESIS; STRUCTURE ACTIVITY RELATION; THERMOBACILLUS XYLANILYTICUS; THERMODYNAMICS; THERMOPHILIC BACTERIUM; WILD TYPE;

AMINO ACID SEQUENCE; BACILLACEAE; BINDING SITES; CATALYSIS; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; GLYCOSIDE HYDROLASES; HYDROGEN; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; MUTATION; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PHENYLALANINE; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; SUBSTRATE SPECIFICITY; THERMODYNAMICS;

THERMOBACILLUS XYLANILYTICUS;

EID: 84866349606     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2012.08720.x     Document Type: Article

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