The X6 'thermostabilizing' domains of xylanases are carbohydrate-binding modules: Structure and biochemistry of the Clostridium thermocellum X6b domain

Biochemistry

Volumn 39, Issue 17, 2000, Pages 5013-5021

  Charnock, Simon J ^a   Bolam, David N ^b   Turkenburg, Johan P ^a   Gilbert, Harry J ^b   Ferreira, Luis M A ^c   Davies, Gideon J ^a   Fontes, Carlos M G A ^c  

^a UNIVERSITY OF YORK   (United Kingdom)

^b NEWCASTLE UNIVERSITY   (United Kingdom)

^c FACULDADE DE MEDICINA VETERINÁRIA   (Portugal)

Author keywords

[No Author keywords available]

Indexed keywords

CARBOHYDRATE; OLIGOSACCHARIDE; POLYSACCHARIDE; TRYPTOPHAN; TYROSINE; XYLAN; XYLAN ENDO 1,3 BETA XYLOSIDASE; XYLOSE;

ARTICLE; CATALYST; CLOSTRIDIUM THERMOCELLUM; CONTROLLED STUDY; ENTHALPY; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME STRUCTURE; HYDROLYSIS; PRIORITY JOURNAL; STRUCTURE ACTIVITY RELATION; STRUCTURE ANALYSIS; THERMOSTABILITY;

BASE SEQUENCE; BINDING SITES; CARBOHYDRATE METABOLISM; CARBOHYDRATES; CLOSTRIDIUM; ENZYME STABILITY; MOLECULAR SEQUENCE DATA; PROTEIN CONFORMATION; SUBSTRATE SPECIFICITY; TEMPERATURE; XYLAN ENDO-1,3-BETA-XYLOSIDASE; XYLOSIDASES;

BACTERIA (MICROORGANISMS); CLOSTRIDIUM THERMOCELLUM;

EID: 0034595226     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi992821q     Document Type: Article

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