Val216 decides the substrate specificity of α-glucosidase in Saccharomyces cerevisiae

European Journal of Biochemistry

Volumn 271, Issue 16, 2004, Pages 3414-3420

  Yamamoto, Keizo ^a   Nakayama, Akifumi ^b   Yamamoto, Yuka ^a   Tabata, Shiro ^a  

^a NARA MEDICAL UNIVERSITY   (Japan)

^b Nara Prefectural Institute for Hygiene and Environment   (Japan)

Author keywords

glucosidase; Family 13; Saccharomyces cerevisiae; Site directed mutagenesis; Substrate specificity

Indexed keywords

ALPHA GLUCOSIDASE; AMYLASE; CHIMERIC PROTEIN; ISOMALTOSE; MALTOSE; OLIGO 1,6 GLUCOSIDASE; VALINE;

ARTICLE; CONSENSUS SEQUENCE; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME SPECIFICITY; ENZYME SUBSTRATE COMPLEX; ESCHERICHIA COLI; EXPRESSION VECTOR; FUNGAL GENE; GENE EXPRESSION; HYDROLYSIS; MOLECULAR CLONING; NONHUMAN; PRIORITY JOURNAL; SACCHAROMYCES CEREVISIAE; SEQUENCE HOMOLOGY; SITE DIRECTED MUTAGENESIS; STRUCTURE ACTIVITY RELATION; X RAY CRYSTALLOGRAPHY;

ALPHA-GLUCOSIDASES; AMINO ACID SEQUENCE; CLONING, MOLECULAR; KINETICS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT FUSION PROTEINS; RECOMBINANT PROTEINS; SACCHAROMYCES CEREVISIAE; SEQUENCE ALIGNMENT; SUBSTRATE SPECIFICITY; VALINE;

ESCHERICHIA COLI; SACCHAROMYCES; SACCHAROMYCES CEREVISIAE; VECTORS;

EID: 4344689082     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.2004.04276.x     Document Type: Article

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