Structural characterization of the bifunctional glucanase-xylanase CelM2 reveals the metal effect and substrate-binding moiety

Biochemical and Biophysical Research Communications

Volumn 391, Issue 4, 2010, Pages 1726-1730

  Nam, Ki Hyun ^a   Lee, Won Ho ^a   Rhee, Kyung Hee ^a   Hwang, Kwang Yeon ^a  

^a Korea University   (South Korea)

Author keywords

CelM2; Glucanase xylanase; Molecular modeling; Substrate binding moiety; Zinc ion binding

Indexed keywords

CAP BINDING PROTEIN; CELLULOSE; CERIUM 144; ENZYME CE1M2; GLUCAN GLUCOSIDASE; GLUCOSE; HYDROXYL GROUP; UNCLASSIFIED DRUG; XYLAN ENDO 1,3 BETA XYLOSIDASE; ZINC ION;

ARTICLE; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME STRUCTURE; ENZYME SUBSTRATE COMPLEX; METAL BINDING; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN FUNCTION; STRUCTURE ANALYSIS;

CATALYSIS; CRYSTALLOGRAPHY, X-RAY; GENE LIBRARY; GLUCOSE; GLYCOSIDE HYDROLASES; METAGENOME; PROTEIN FOLDING; SUBSTRATE SPECIFICITY; ZINC;

EID: 74449089600     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2009.12.141     Document Type: Article

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