Role of subsite +1 residues in pH dependence and catalytic activity of the glycoside hydrolase family 1 β-glucosidase BGL1A from the basidiomycete Phanerochaete chrysosporium

Biotechnology and Bioengineering

Volumn 99, Issue 6, 2008, Pages 1295-1302

  Tsukada, Takeshi ^a   Igarashi, Kiyohiko ^a   Fushinobu, Shinya ^a   Samejima, Masahiro ^a  

^a UNIVERSITY OF TOKYO   (Japan)

Author keywords

glucosidase; Cellobiose; Enzymatic saccharification; Glycoside hydrolase; Phanerochaete chrysosporium

Indexed keywords

BASIDIOMYCETE PHANEROCHAETE CHRYSOSPORIUM; ENZYMATIC SACCHARIFICATION; GLYCOSIDE HYDROLASE; PHANEROCHAETE CHRYSOSPORIUM;

AMINO ACIDS; CATALYST ACTIVITY; ENZYME KINETICS; KINETIC PARAMETERS; PH EFFECTS;

FUNGI;

1 BETA GLUCOSIDASE; 1 BETA GLUCOSIDASE BGL1A; 1 BETA GLUCOSIDASE BGL1B; CELLOBIOSE; D229 ENZYME; ENZYME; GLYCOSIDASE; K253 ENZYME; UNCLASSIFIED DRUG; BETA GLUCOSIDASE;

AMINO ACID SEQUENCE; ARTICLE; BASIDIOMYCETES; CATALYSIS; CONTROLLED STUDY; GENE MUTATION; HYDROLYSIS; KINETICS; NONHUMAN; NUCLEOTIDE SEQUENCE; PH; PHANEROCHAETE; AMINO ACID SUBSTITUTION; CHEMISTRY; ENZYME ACTIVATION; ENZYME STABILITY; ENZYMOLOGY; GENETICS; METABOLISM; METHODOLOGY; PROTEIN ENGINEERING; SITE DIRECTED MUTAGENESIS; STRUCTURE ACTIVITY RELATION;

PHANEROCHAETE CHRYSOSPORIUM;

AMINO ACID SUBSTITUTION; BETA-GLUCOSIDASE; CATALYSIS; ENZYME ACTIVATION; ENZYME STABILITY; HYDROGEN-ION CONCENTRATION; MUTAGENESIS, SITE-DIRECTED; PHANEROCHAETE; PROTEIN ENGINEERING; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 41049100848     PISSN: 00063592     EISSN: 10970290     Source Type: Journal    
DOI: 10.1002/bit.21717     Document Type: Article

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