Probing the role of tightly bound phosphoenolpyruvate in Escherichia coli 3-deoxy- d- manno-octulosonate 8-phosphate synthase catalysis using quantitative time-resolved electrospray ionization mass spectrometry in the millisecond time range

Escherichia coli 3-deoxy- d- manno-octulosonate 8-phosphate (KDO8P) synthase catalyzes the condensation of phosphoenolpyruvate (PEP) and d-arabinose 5-phosphate (A5P) to produce KDO8P and inorganic phosphate. The enzyme is often isolated with varying amounts of tightly bound PEP substrate. To better...

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Veröffentlicht in:	Analytical biochemistry 2005-08, Vol.343 (1), p.35-47
Hauptverfasser:	Li, Zhili, Sau, Apurba K., Furdui, Cristina M., Anderson, Karen S.
Format:	Artikel
Sprache:	eng
Schlagworte:	Aldehyde-Lyases - chemistry Catalysis E. coli 3-deoxy- d- manno-octulosonate 8-phosphate synthase Electrospray ionization mass spectrometry Escherichia coli Escherichia coli - enzymology Escherichia coli Proteins - chemistry Kinetics Phosphoenolpyruvate Phosphoenolpyruvate - chemistry Rapid chemical quench Spectrometry, Mass, Electrospray Ionization - methods Time Transient kinetics
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