Inactivation of Escherichia coli threonine synthase by DL-Z-2-amino-5-phosphono-3-pentenoic acid.
The rhizocticines and plumbemicines are two groups of di- and tripeptid antibiotics thought to interfere with threonine or threonine-related metabolism. Z-2-amino-5-phosphono-3-pentenoic acid, the common unusual amino acid constituent of the rhizocticines and plumbemicines, was found to irreversibly inhibit Escherichia coli threonine synthase in a time-dependent reaction that followed pseudo-first order and saturation kinetics. These data provide evidence that the toxicity of the rhizocticines and plumbemicines is due to the inhibition of threonine synthase by Z-2-amino-5-phosphone-3-pentenoic acid, which is liberated by peptidases after uptake into the target cell. Additionally, methods for the purification of threonine synthase from an overproducing E. coli strain and for the enzymatic synthesis of L-homoserine phosphate are described.
Laber
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Schering AG, Berlin, Germany.
Lindell
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Pohlenz
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D019757:Carbon-Oxygen Lyases; D004926:Escherichia coli / Q000201:enzymology*; D008190:Lyases / Q000037:antagonists & inhibitors*; D013997:Time Factors; D014633:Valine / Q000031:analogs & derivatives* / Q000494:pharmacology
C056639:2-amino-5-phosphopentanoic acid; D008190:Lyases; D019757:Carbon-Oxygen Lyases; C023160:threonine synthase; D014633:Valine