β-Galactosidase (Escherichia coli) has a second catalytically important Mg2+ site

It is shown here that Escherichia coli β-galactosidase has a second Mg2+ binding site that is important for activity. Binding of Mg2+ to the second site caused the kcat (with oNPG as the substrate) to increase about 100s−1; the Km was not affected. The Kd for binding the second Mg2+ is about 10−4M....

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Veröffentlicht in:	Biochemical and biophysical research communications 2007-01, Vol.352 (2), p.566-570
Hauptverfasser:	Sutendra, Gopinath, Wong, Sean, Fraser, Marie E., Huber, Reuben E.
Format:	Artikel
Sprache:	eng
Schlagworte:	beta-Galactosidase - chemistry Binding Sites Catalysis Entropy Enzyme Activation Escherichia coli - enzymology Magnesium - chemistry Mg2 Protein Binding Transition state binding β-Galactosidase
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