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Overexpression, Purification, and Use of Phosphoenol Pyruvate Synthetase in the Synthesis of PEP Analogues

✍ Scribed by David L. Jakeman; Jeremy N.S. Evans

Publisher
Elsevier Science
Year
1998
Tongue
English
Weight
276 KB
Volume
26
Category
Article
ISSN
0045-2068

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✦ Synopsis

The Escherichia coli enzyme phosphoenol pyruvate synthetase has been overexpressed and purified in a single chromatographic step. The enzyme catalyzes the synthesis of phosphoenol pyruvate (PEP), from adenosine triphosphate and pyruvate, and has enabled the synthesis of uniformly labeled [1,2,3-13 C 3 ]PEP, which is a key molecule in structural and mechanistic studies of enolpyruvyl transferases. Fluoropyruvate was also used as substrate for the enzyme and gave only (Z)-phoephoenol-3-fluoropyruvate, albeit at a slower rate.

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