Structure-function relationships for Schizophyllum commune trehalose phosphorylase and their implications for the catalytic mechanism of family GT-4 glycosyltransferases

Biochemical Journal

Volumn 397, Issue 3, 2006, Pages 491-500

  Goedl, Christiane ^a   Griessler, Richard ^a   Schwarz, Alexandra ^a   Nidetzky, Bernd ^a  

^a GRAZ UNIVERSITY OF TECHNOLOGY   (Austria)

Author keywords

retaining mechanism; Fold family GT B; Glycosyltransferase; Internal return mechanism; Schizophyllum commune; Trehalose phosphorylase

Indexed keywords

AMINO ACIDS; CATALYSTS; DIMERS; DNA; ESCHERICHIA COLI; FUNGI; HYDROLYSIS; IONS; PROTEINS; SUBSTRATES;

Α-RETAINING MECHANISM; FOLD FAMILY GT-B; GLYCOSYLTRANSFERASE; INTERNAL RETURN MECHANISM; SCHIZOPHYLLUM COMMUNE; TREHALOSE PHOSPHORYLASE;

ENZYMES;

AMINO ACID; ARGININE; ASPARTIC ACID; DIMER; GLYCOSYLTRANSFERASE; HISTIDINE; LYSINE; MAGNESIUM ION; PHOSPHORYLASE; PROTEIN SCTPASE; RECOMBINANT PROTEIN; TREHALOSE; UNCLASSIFIED DRUG; VALIDOXYLAMINE A;

ARTICLE; CATALYSIS; CONTROLLED STUDY; DEPHOSPHORYLATION; HYDROLYSIS; MASS SPECTROMETRY; MOLECULAR CLONING; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN ISOLATION; PROTEIN PURIFICATION; SCHIZOPHYLLUM COMMUNE; SEQUENCE ANALYSIS; SITE DIRECTED MUTAGENESIS; STRUCTURE ACTIVITY RELATION;

AMINO ACID SEQUENCE; BINDING SITES; CATALYSIS; ESCHERICHIA COLI; GLUCOSYLTRANSFERASES; GLYCOSYLTRANSFERASES; KINETICS; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; POINT MUTATION; PROTEIN CONFORMATION; RECOMBINANT PROTEINS; SCHIZOPHYLLUM; STRUCTURE-ACTIVITY RELATIONSHIP;

ESCHERICHIA COLI; FUNGI; SCHIZOPHYLLUM COMMUNE;

EID: 33746882419     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20060029     Document Type: Article

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