Catalytic mechanism of α-retaining glucosyl transfer by Corynebacterium callunae starch phosphorylase: The role of histidine-334 examined through kinetic characterization of site-directed mutants

Biochemical Journal

Volumn 387, Issue 2, 2005, Pages 437-445

  Schwarz, Alexandra ^a   Pierfederici, Francesco Maria ^a   Nidetzky, Bernd ^a  

^a GRAZ UNIVERSITY OF TECHNOLOGY   (Austria)

Author keywords

Corynebacterium callunae; Glycogen phosphorylase; Glycosyltransferase; Maltodextrin; Retaining mechanism; Site directed mutagenesis

Indexed keywords

AMINO ACIDS; BACTERIA; ENZYMES; FLUORESCENCE; MUTAGENESIS; PHOSPHATES; QUENCHING; STARCH;

LIGANDS; MUTANTS; PHOSPHOROLYSIS; TRANSITION STATES;

CATALYSIS;

1,4 ALPHA GLUCAN BRANCHING ENZYME; ALPHA GLUCAN; GLUCAN; GLUCONOLACTONE; GLUCOSE; GLUCOSE 1 PHOSPHATE; HISTIDINE; LACTONE; PYRIDOXAL 5 PHOSPHATE; STARCH; STARCH PHOSPHORYLASE; UNCLASSIFIED DRUG; XYLOSE; XYLOSE 1 PHOSPHATE;

AMINO ACID SEQUENCE; ARTICLE; COMPLEX FORMATION; CONTROLLED STUDY; CORYNEBACTERIUM; CORYNEBACTERIUM CALLUNAE; DISSOCIATION; ENZYME ACTIVE SITE; ENZYME BINDING; ENZYME KINETICS; ENZYME MECHANISM; FLUORESCENCE; NONHUMAN; PH; PRIORITY JOURNAL; PROTEIN BINDING; SITE DIRECTED MUTAGENESIS; TEMPERATURE; WILD TYPE;

AMINO ACID SEQUENCE; BINDING SITES; CATALYSIS; CORYNEBACTERIUM; GLUCONATES; GLUCOSE; HISTIDINE; KINETICS; MODELS, CHEMICAL; MUTAGENESIS, SITE-DIRECTED; PHOSPHORYLATION; PROTEIN BINDING; STARCH PHOSPHORYLASE;

EID: 17644368570     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20041593     Document Type: Article

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