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

FEBS Letters

Auger, Geneviève¹  van Heijenoort, Jean¹  Blanot, Didier¹  Vederas, John C.² 

[1] URA 1131 du CNRS, Biochemie Moléculaire et Cellulaire, Bâtiment 432, Université de Paris-Sud 91405 Orsay, France;Department of Chemistry, University of Alberta, Edmonton, Alberta T6G 2G2, Canada

关键词: meso-Diaminopimelate-adding enzyme;    Diaminopimelic acid analog;    MurE;    Peptidoglycan biosynthesis;    A2pm;    2;    6-diaminopimelic acid;    DapF;    ll-2;    6-diaminopimelate 2-epimerase;    LysA;    meso-2;    6-diaminopimelate carboxylyase;    MurE;    meso-2;    6-diaminopimelate ligase (ADP-forming);    MurNAc;    N-acetylmuramoryl;   

DOI  :  10.1016/0014-5793(96)00619-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown