Homologous xylanases from Clostridium thermocellum: Evidence for bi-functional activity, synergism between xylanase catalytic modules and the presence of xylan-binding domains in enzyme complexes

Biochemical Journal

Volumn 342, Issue 1, 1999, Pages 105-110

  Fernandes, Ana C ^a   Fontes, Carlos M G A ^a   Gilbert, Harry J ^b   Hazlewood, Geoffrey P ^c   Fernandes, Tito H ^a   Ferreira, Luis M A ^a  

^a FACULDADE DE MEDICINA VETERINÁRIA   (Portugal)

^b NEWCASTLE UNIVERSITY   (United Kingdom)

^c BABRAHAM INSTITUTE   (United Kingdom)

Author keywords

Carbohydrate binding domain; Xylan deacetylation

Indexed keywords

ACETIC ACID DERIVATIVE; BACTERIAL ENZYME; CELLULOSE; GLYCOSIDASE; MICROCRYSTALLINE CELLULOSE; MUTANT PROTEIN; POLYSACCHARIDE; PROTEIN DERIVATIVE; XYLAN; XYLAN ENDO 1,3 BETA XYLOSIDASE;

AMINO ACID SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CATALYSIS; CLOSTRIDIUM THERMOCELLUM; CONTROLLED STUDY; DEACETYLATION; ENZYME ACTIVITY; ENZYME BINDING; HYDROLYSIS; MOLECULAR CLONING; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN STABILITY; SEQUENCE HOMOLOGY; STRUCTURE ACTIVITY RELATION; THERMOSTABILITY;

ACETYLATION; AMIDOHYDROLASES; BACTERIAL PROTEINS; BINDING SITES; CATALYTIC DOMAIN; CELLULOSE; CLONING, MOLECULAR; CLOSTRIDIUM; ENZYME STABILITY; GENES, BACTERIAL; HYDROGEN-ION CONCENTRATION; HYDROLYSIS; KINETICS; LIGANDS; MULTIENZYME COMPLEXES; SEQUENCE DELETION; SEQUENCE HOMOLOGY, AMINO ACID; SOLUBILITY; SUBSTRATE SPECIFICITY; TEMPERATURE; XYLAN ENDO-1,3-BETA-XYLOSIDASE; XYLANS; XYLOSIDASES;

BACTERIA (MICROORGANISMS); CLOSTRIDIUM THERMOCELLUM;

EID: 0033567339     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/0264-6021:3420105     Document Type: Article

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