Probing the active site of Corynebacterium callunae starch phosphorylase through the characterization of wild-type and His334→Gly mutant enzymes

FEBS Journal

Volumn 274, Issue 19, 2007, Pages 5105-5115

  Schwarz, Alexandra ^a   Brecker, Lothar ^b   Nidetzky, Bernd ^a  

^a GRAZ UNIVERSITY OF TECHNOLOGY   (Austria)

^b UNIVERSITY OF VIENNA   (Austria)

Author keywords

retaining glucosyl transfer; Phosphorus NMR; Pyridoxal 5 phosphate; Saturation transfer difference NMR; Starch phosphorylase

Indexed keywords

ALPHA DEXTRO GLUCOSE 1 PHOSPHATE; ALPHA DEXTRO XYLOSE 1 PHOSPHATE; ARSENIC ACID; GLYCINE; HISTIDINE; IMIDAZOLE; PHOSPHATE; PHOSPHORYLASE; PYRIDOXAL 5 PHOSPHATE; STARCH PHOSPHORYLASE; UNCLASSIFIED DRUG;

ARTICLE; BINDING AFFINITY; CATALYSIS; CONTROLLED STUDY; CORYNEBACTERIUM; CORYNEBACTERIUM CALLUNAE; ENZYME ACTIVITY; ENZYME STRUCTURE; ENZYME SUBSTRATE; HYDROGEN BOND; LIGAND BINDING; MUTATIONAL ANALYSIS; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PH MEASUREMENT; PHOSPHORUS NUCLEAR MAGNETIC RESONANCE; POINT MUTATION; PRIORITY JOURNAL; PROTEIN PURIFICATION; PROTON NUCLEAR MAGNETIC RESONANCE; STEADY STATE; WILD TYPE;

BASE SEQUENCE; BINDING SITES; CORYNEBACTERIUM; DNA PRIMERS; GLYCINE; HISTIDINE; HYDROGEN-ION CONCENTRATION; KINETICS; LIGANDS; MODELS, MOLECULAR; MOLECULAR PROBES; MUTAGENESIS, SITE-DIRECTED; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN BINDING; STARCH PHOSPHORYLASE;

CORYNEBACTERIUM CALLUNAE;

EID: 34748824093     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2007.06030.x     Document Type: Article

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