Purification and characterization of phosphoenolpyruvate phosphomutase from Pseudomonas gladioli B-1.

Abstract

Phosphoenolpyruvate phosphomutase (PEPPM) catalyzes C-P bond formation by intramolecular rearrangement of phosphoenolpyruvate to phosphonopyruvate (PnPy). We purified PEPPM from a gram-negative bacterium, Pseudomonas gladioli B-1 isolated as a C-P compound producer. The equilibrium of this reaction favors the formation of the phosphate ester by cleaving the… (More)

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@article{Nakashita1992PurificationAC, title={Purification and characterization of phosphoenolpyruvate phosphomutase from Pseudomonas gladioli B-1.}, author={Harumi Nakashita and Atsushi Shimazu and Toshirou Hidaka and Hideki Seto}, journal={Journal of bacteriology}, year={1992}, volume={174 21}, pages={6857-61} }