Substrate binding to fluorescent labeled wild type, Lys213Arg, and His233Gln Saccharomyces cerevisiae phosphoenolpyruvate carboxykinases

Saccharomyces cerevisiae phosphoenolpyruvate (PEP) carboxykinase is a key enzyme of the gluconeogenic pathway and catalyzes the decarboxylation of oxaloacetate and transfer of the γ-phosphoryl group of ATP to yield PEP, ADP, and CO 2 in the presence of a divalent metal ion. Previous experiments have...

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Veröffentlicht in:	The international journal of biochemistry & cell biology 2004-05, Vol.36 (5), p.861-869
Hauptverfasser:	Bueno, Claudia, González-Nilo, Fernando D., Victoria Encinas, Marı́a, Cardemil, Emilio
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Substitution Homology modeling Ligand binding Mutation Phosphoenolpyruvate - metabolism Phosphoenolpyruvate Carboxykinase (ATP) - chemistry Phosphoenolpyruvate Carboxykinase (ATP) - genetics Phosphoenolpyruvate Carboxykinase (ATP) - metabolism Phosphopyridoxyl fluorescence spectroscopy Protein Binding S. cerevisiae phosphoenolpyruvate carboxykinase Saccharomyces cerevisiae - enzymology Spectrometry, Fluorescence Staining and Labeling Structural Homology, Protein Substrate Specificity
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