How family 26 glycoside hydrolases orchestrate catalysis on different polysaccharides: Structure and activity of a Clostridium thermocellum lichenase, CtLic26A

Journal of Biological Chemistry

Volumn 280, Issue 38, 2005, Pages 32761-32767

  Taylor, Edward J ^a   Goyal, Arun ^b,f   Guerreiro, Catarina I P D ^b   Prates, José A M ^b   Money, Victoria A ^a   Ferry, Natalie ^c   Morland, Carl ^c   Planas, Antoni ^d   Macdonald, James A ^e   Stick, Robert V ^e   Gilbert, Harry J ^c   Fontes, Carlos M G A ^b   Davies, Gideon J ^a  

^a UNIVERSITY OF YORK   (United Kingdom)

^b UNIVERSITY OF LISBON   (Portugal)

^c NEWCASTLE UNIVERSITY   (United Kingdom)

^d INSTITUT QUÍMIC DE SARRIÀ   (Spain)

^e UNIVERSITY OF WESTERN AUSTRALIA   (Australia)

^f INDIAN INSTITUTE OF TECHNOLOGY GUWAHATI   (India)

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMISTRY; CATALYSIS; MOLECULAR BIOLOGY; MOLECULAR STRUCTURE; ORGANIC POLYMERS; POLYSACCHARIDES; XYLOSE;

CATALYTIC APPARATUS; HOMOPOLYMERS; LICHENAN-BASED SUBSTRATES; SUBSTRATE RECOGNITION;

ENZYMES;

ACID; BACTERIAL ENZYME; BASE; BETA 1,4 MANNANASE; BETA MANNOSIDASE; CTLIC26A PROTEIN; GLUCOSE POLYMER; GLUCOSIDE; GLYCOSIDASE; LICHENASE; MANNOSE; OLIGOSACCHARIDE; OXYGEN; POLYMER; POLYSACCHARIDE; UNCLASSIFIED DRUG; XYLOSE;

ARTICLE; CATALYSIS; CLOSTRIDIUM THERMOCELLUM; CONFORMATION; ENZYME ACTIVITY; ENZYME MECHANISM; ENZYME SPECIFICITY; ENZYME STRUCTURE; ENZYME SUBSTRATE; HYDROLYSIS; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN FAMILY; PROTON TRANSPORT;

BINDING, COMPETITIVE; CATALYSIS; CLONING, MOLECULAR; CLOSTRIDIUM THERMOCELLUM; CRYSTALLOGRAPHY, X-RAY; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ESCHERICHIA COLI; GLUCOSE; GLYCOSIDE HYDROLASES; HYDROGEN BONDING; HYDROGEN-ION CONCENTRATION; HYDROLYSIS; KINETICS; MANNOSE; MODELS, CHEMICAL; MODELS, MOLECULAR; POLYMERS; POLYSACCHARIDES; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT PROTEINS; SUBSTRATE SPECIFICITY; XYLOSE;

CLOSTRIDIUM THERMOCELLUM;

EID: 25444476150     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M506580200     Document Type: Article

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