Inhibition of the two-subsite β-d-xylosidase from Selenomonas ruminantium by sugars: Competitive, noncompetitive, double binding, and slow binding modes

Archives of Biochemistry and Biophysics

Volumn 465, Issue 1, 2007, Pages 231-246

  Jordan, Douglas B ^a   Braker, Jay D ^a  

^a NATIONAL CENTER FOR AGRICULTURAL UTILIZATION RESEARCH   (United States)

Author keywords

l Arabinofuranosidase; GH43; Glycoside hydrolase; Hemicellulose; Hysteresis; Saccharification; Structure function

Indexed keywords

ARABINOSE; BIOFUEL; ENZYME INHIBITOR; HYDROLASE; SUGAR; XYLAN 1,4 BETA XYLOSIDASE; XYLOSE;

ARTICLE; BINDING AFFINITY; BIOMASS; CATALYSIS; COMPLEX FORMATION; FERMENTATION; NONHUMAN; PRIORITY JOURNAL; PROTON TRANSPORT; SACCHARIFICATION; SELENOMONAS RUMINANTIUM;

BINDING SITES; BLOOD PROTEINS; CARBOHYDRATES; COMPUTER SIMULATION; ENZYME ACTIVATION; ENZYME INHIBITORS; KINETICS; MODELS, CHEMICAL; MODELS, MOLECULAR; PROTEIN BINDING; SELENOMONAS; SUBSTRATE SPECIFICITY; XYLOSIDASES;

SELENOMONAS RUMINANTIUM;

EID: 34548039761     PISSN: 00039861     EISSN: 10960384     Source Type: Journal    
DOI: 10.1016/j.abb.2007.05.016     Document Type: Article

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