Issue 7, 2006

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

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

Article information

Article type
Communication
Submitted
16 Dec 2005
Accepted
14 Feb 2006
First published
01 Mar 2006

Org. Biomol. Chem., 2006,4, 1209-1212

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

D. Alexeev, Robert. L. Baxter, D. J. Campopiano, O. Kerbarh, L. Sawyer, N. Tomczyk, R. Watt and S. P. Webster, Org. Biomol. Chem., 2006, 4, 1209 DOI: 10.1039/B517922J

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