The 184th residue of β-glucosidase Bgl1B plays an important role in glucose tolerance

Journal of Bioscience and Bioengineering

Volumn 112, Issue 5, 2011, Pages 447-450

  Liu, Juanjuan ^a,b   Zhang, Xuecheng ^a,b   Fang, Zemin ^a,b,c   Fang, Wei ^a,b   Peng, Hui ^a,b   Xiao, Yazhong ^a,b  

^a ANHUI UNIVERSITY   (China)

^b Anhui Provincial Engineering Technology Research Center of Microorganisms and Biocatalysis   (China)

^c INSTITUTE OF GEOLOGY AND GEOPHYSICS   (China)

Author keywords

Glucosidase; Competitive inhibition; GH1; Glucose tolerance; Mutation

Indexed keywords

COMPETITIVE INHIBITION; GH1; GLUCOSE TOLERANCE; GLUCOSIDASE; MUTATION;

AMINO ACIDS;

GLUCOSE;

BACTERIAL PROTEIN; BETA GLUCOSIDASE; GLUCOPYRANOSIDE; GLUTAMIC ACID; PHENYLALANINE; PROTEIN BGL1B; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; BACTERIAL STRAIN; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME STABILITY; ESCHERICHIA COLI; GLUCOSE TOLERANCE; MUTATION; NONHUMAN; PAENIBACILLUS POLYMYXA; PH; POLYMERASE CHAIN REACTION; PROTEIN FUNCTION; PROTEIN STRUCTURE; SEQUENCE ANALYSIS; SITE DIRECTED MUTAGENESIS; STRUCTURE ANALYSIS; WILD TYPE;

AMINO ACID SUBSTITUTION; BETA-GLUCOSIDASE; ENZYME STABILITY; KINETICS; METAGENOMICS; MUTAGENESIS, SITE-DIRECTED; PAENIBACILLUS; SUBSTRATE SPECIFICITY;

PAENIBACILLUS POLYMYXA;

EID: 81255135961     PISSN: 13891723     EISSN: 13474421     Source Type: Journal    
DOI: 10.1016/j.jbiosc.2011.07.017     Document Type: Article

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