Examination of the thiamin diphosphate binding site in yeast transketolase by site-directed mutagenesis

The role of two conserved amino acid residues in the thiamin diphosphate binding site of yeast transketolase has been analyzed by site-directed mutagenesis. Replacement of E162, which is part of a cluster of glutamic acid residues at the subunit interface, by alanine or glutamine results in mutant e...

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Veröffentlicht in:	European journal of biochemistry 1997-03, Vol.244 (2), p.646-652
Hauptverfasser:	Meshalkina, L, Nilsson, U, Wikner, C, Kostikowa, T, Schneider, G
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Binding Sites - genetics Circular Dichroism Conserved Sequence Crystallography, X-Ray Dimerization Electrochemistry enzyme mechanism Enzyme Stability Kinetics Medicin och hälsovetenskap Models, Molecular Molecular Structure Mutagenesis, Site-Directed Protein Conformation protein crystallography Saccharomyces cerevisiae Saccharomyces cerevisiae - enzymology Saccharomyces cerevisiae - genetics site‐directed mutagenesis thiamin diphosphate Thiamine Pyrophosphate - metabolism transketolase Transketolase - genetics Transketolase - metabolism
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