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Aminoalkylphosphinate inhibitors of D-Ala-D-Ala adding enzyme

Miller, David James, Hammond, Stephen M., Anderluzzi, Daniela and Bugg, Timothy D. H. 1998. Aminoalkylphosphinate inhibitors of D-Ala-D-Ala adding enzyme. Journal of the Chemical Society, Perkin Transactions 1 (1) , pp. 131-132. 10.1039/a704097k

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Pseudo-tri- and -tetra-peptide aminoalkylphosphinic acids of general structure X-Lys-PO2H-Gly-Ala have been synthesised as transition state analogues for D-Ala-D-Ala adding enzyme. The key synthetic step used to assemble the C-terminal dipeptide unit is a modified Arbusov reaction, coupling bromopropionyl-D-alanine methyl ester to a silylated aminoalkylphosphonite. Kinetic assays with the purified E. coli enzyme reveal that the phosphinate analogues act as reversible competitive inhibitors, with Ki values in the range 200–700 µ>M>. Extended analogues mimicking the peptide chain of the UDPMurNAc-L-Ala-γ-D-Glu-m-DAP substrate show increased binding affinity for the enzyme active site. These are the first reported inhibitors for D-Ala-D-Ala adding enzyme.

Item Type: Article
Status: Published
Schools: Chemistry
Subjects: Q Science > QD Chemistry
Publisher: RSC Publishing
ISSN: 0300-922X
Last Modified: 04 Jun 2017 02:50

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