Variation in relative substrate specificity of bifunctional β-d-xylosidase/α-l-arabinofuranosidase by single-site mutations: Roles of substrate distortion and recognition

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1774, Issue 9, 2007, Pages 1192-1198

  Jordan, Douglas B ^a   Li, Xin Liang ^a  

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

Author keywords

GH43; Glycoside hydrolase; Near attack conformation; Stereoelectronic effect; Transition state

Indexed keywords

4 NITROPHENYL ALPHA L ARABINOFURASONIDE; 4 NITROPHENYL BETA D XYLOPYRANOSIDE; ALANINE; ALPHA ARABINOFURANOSIDASE; UNCLASSIFIED DRUG; XYLAN 1,4 BETA XYLOSIDASE;

ARTICLE; CATALYSIS; CONTROLLED STUDY; ENZYME KINETICS; ENZYME SPECIFICITY; GENE MUTATION; GENETIC VARIABILITY; HYDROLYSIS; NONHUMAN; PRIORITY JOURNAL; SEGREGATION DISTORTION; SELENOMONAS RUMINANTIUM; SITE DIRECTED MUTAGENESIS; STEADY STATE;

BINDING SITES; GLYCOSIDE HYDROLASES; HYDROGEN-ION CONCENTRATION; KINETICS; MODELS, MOLECULAR; SUBSTRATE SPECIFICITY; XYLOSIDASES;

SELENOMONAS RUMINANTIUM;

EID: 34548249519     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2007.06.010     Document Type: Article

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