Evidence that GH115 α-glucuronidase activity, which is required to degrade plant biomass, is dependent on conformational flexibility

Journal of Biological Chemistry

Volumn 289, Issue 1, 2014, Pages 53-64

  Rogowski, Artur ^a   Baslé, Arnaud ^a   Farinas, Cristiane S ^b,c   Solovyova, Alexandra ^a   Mortimer, Jennifer C ^b   Dupree, Paul ^b   Gilbert, Harry J ^a   Bolam, David N ^a  

^a NEWCASTLE UNIVERSITY   (United Kingdom)

^b UNIVERSITY OF CAMBRIDGE   (United Kingdom)

^c EMBRAPA CERRADOS   (Brazil)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BIODEGRADATION; CHAINS; CRYSTAL STRUCTURE; PLANTS (BOTANY); PROTEINS; SUBSTRATES;

BIOLOGICAL PROCESS; CONFORMATIONAL CHANGE; CONFORMATIONAL FLEXIBILITY; GLYCOSIDE HYDROLASES; METHYLGLUCURONIC ACIDS; MICROBIAL DEGRADATION; POTENTIAL SUBSTRATE; PROTEIN DIMERIZATION;

ENZYME ACTIVITY;

GH115 PROTEIN; GLYCOSIDASE; UNCLASSIFIED DRUG; ALPHA-GLUCURONIDASE; BACTERIAL PROTEIN; GLUCURONOXYLAN; XYLAN;

ARTICLE; BIODEGRADATION; CARBOXY TERMINAL SEQUENCE; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVITY; ENZYME CONFORMATION; ENZYME STRUCTURE; ENZYME SUBSTRATE; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN DOMAIN; STRUCTURE ACTIVITY RELATION; STRUCTURE ANALYSIS; BACTEROIDES; BIOMASS; CHEMISTRY; ENZYME SPECIFICITY; ENZYMOLOGY; HUMAN; PLANT; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; X RAY CRYSTALLOGRAPHY;

BACTERIAL PROTEINS; BACTEROIDES; BIOMASS; CRYSTALLOGRAPHY, X-RAY; GLYCOSIDE HYDROLASES; HUMANS; PLANTS; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SUBSTRATE SPECIFICITY; XYLANS;

EID: 84891721633     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.525295     Document Type: Article

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