Effect of analogues of diaminopimelic acid on the meso‐diaminopimelate‐adding enzyme from Escherichia coli

Abstract
Several analogues of diaminopimelic acid (A2pm) were tested as substrates or inhibitors of the meso‐diaminopimelate‐adding enzyme from Escherichia coli. They included lanthionine derivatives, a phosphonic analogue, heterocyclic compounds, 3‐fluoro‐A2pm, 4‐methylene‐A2pm and N‐hydroxy‐A2pm. The best substrates were, in decreasing order of specific enzyme activity, (2S,3R,6S)‐3‐fluoro‐A2pm, meso‐lanthionine sulfoxide and N‐hydroxy‐A2pm (mixture of stereoisomers). In those cases where all the stereoisomers were available, the specificity could be described as meso ⪢ DD ≈ LL. N‐Hydroxy‐A2pm (mixture of stereoisomers) strongly inhibited the addition of radioactive meso‐A2pm to UDP‐N‐acetylmuramoyl‐dipeptide.

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