α-retaining glucosyl transfer catalysed by trehalose phosphorylase from Schizophyllum commune: Mechanistic evidence obtained from steady-state kinetic studies with substrate analogues and inhibitors

Biochemical Journal

Volumn 360, Issue 3, 2001, Pages 727-736

  Nidetzky, B ^a   Els, C ^a  

^a UNIVERSITY OF NATURAL RESOURCES AND LIFE SCIENCES   (Austria)

Author keywords

Family 4; Glycosyltransferase; Intermediate; Retaining mechanism

Indexed keywords

ENZYME INHIBITION; ENZYMES; POSITIVE IONS;

ANOMERIC CONFIGURATION;

BIOCHEMISTRY;

FUNGAL ENZYME; GLYCOSYLTRANSFERASE; PHOSPHORYLASE; TREHALOSE; VANADIC ACID;

ARTICLE; BASIDIOMYCETES; CATALYSIS; ENZYME ACTIVITY; ENZYME KINETICS; HYDROGEN BOND; NONHUMAN; PRIORITY JOURNAL; SCHIZOPHYLLUM COMMUNE; STEADY STATE;

BINDING SITES; ENZYME INHIBITORS; GLUCOSE; GLUCOSYLTRANSFERASES; GLYCOSYLATION; KINETICS; SCHIZOPHYLLUM; SUBSTRATE SPECIFICITY; VANADATES;

BASIDIOMYCOTA; FUNGI; SCHIZOPHYLLUM; SCHIZOPHYLLUM COMMUNE;

EID: 0035893762     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/0264-6021:3600727     Document Type: Article

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