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Suicide inhibition of α-oxamine synthases: structures of the covalent adducts of 8-amino-7-oxononanoate synthase with trifluoroalanine
Dmitriy Alexeev,Robert. L. Baxter,Dominic J. Campopiano,Olivier Kerbarh,Lindsay Sawyer,Nicholas Tomczyk,Rory Watt,Scott P. Webster
Organic & Biomolecular Chemistry Pub Date : 03/01/2006 00:00:00 , DOI:10.1039/B517922J
Abstract

The irreversible inhibition of 8-amino-7-oxononanoate synthase by trifluoroalanine involves decarboxylative defluorination of the inhibitor-PLP aldimine followed by attack of the conjugated imine by the amino group of the active site lysine to afford a covalently bound difluorinated intermediate which can subsequently undergo further HF losses and hydrolysis to afford a 2-(pyridoximine phosphate) acetoyl protein adduct.

Graphical abstract: Suicide inhibition of α-oxamine synthases: structures of the covalent adducts of 8-amino-7-oxononanoate synthase with trifluoroalanine
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