Structure of a novel thermostable GH51 α-L-arabinofuranosidase from Thermotoga petrophila RKU-1

Protein Science

Volumn 20, Issue 9, 2011, Pages 1632-1637

  Souza, Tatiana A C B ^a   Santos, Camila R ^a   Souza, Angelica R ^a   Oldiges, Daiane P ^a   Ruller, Roberto ^b   Prade, Rolf A ^c   Squina, Fabio M ^b   Murakami, Mario T ^a  

^a BRAZILIAN CENTER FOR RESEARCH IN ENERGY AND MATERIALS CNPEM   (Brazil)

^b BRAZILIAN CENTER FOR RESEARCH IN ENERGY AND MATERIALS CNPEM   (Brazil)

^c OKLAHOMA STATE UNIVERSITY   (United States)

Author keywords

Glycosyl hydrolase family 51; Oligomerization; Structure; Thermostable L arabinofuranosidase; Thermotoga petrophila RKU 1

Indexed keywords

ALPHA ARABINOFURANOSIDASE; DIMER; GH 51 ALPHA LEVO ARABINOFURANOSIDASE; UNCLASSIFIED DRUG;

ANIMAL CELL; ARTICLE; BACTERIAL STRAIN; BETA SHEET; CARBOXY TERMINAL SEQUENCE; CATALYSIS; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME STRUCTURE; HYDROPHOBICITY; NONHUMAN; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN MOTIF; PROTEIN STABILITY; PROTEIN TERTIARY STRUCTURE; ROOM TEMPERATURE; SEQUENCE ANALYSIS; SOLUTION AND SOLUBILITY; THERMOSTABILITY; THERMOTOGA; THERMOTOGA PETROPHILA; X RAY CRYSTALLOGRAPHY;

BACTERIA; BACTERIAL PROTEINS; ENZYME STABILITY; GLYCOSIDE HYDROLASES; MOLECULAR SEQUENCE DATA; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SUBSTRATE SPECIFICITY; TEMPERATURE;

THERMOTOGA; THERMOTOGA PETROPHILA;

EID: 84860389042     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.693     Document Type: Article

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