Crystal structure of a complex between the Actinomadura R39 DD-peptidase and a peptidoglycan-mimetic boronate inhibitor: interpretation of a transition state analogue in terms of catalytic mechanism.

@article{Dzhekieva2010CrystalSO,
  title={Crystal structure of a complex between the Actinomadura R39 DD-peptidase and a peptidoglycan-mimetic boronate inhibitor: interpretation of a transition state analogue in terms of catalytic mechanism.},
  author={Liudmila Alekseyevna Dzhekieva and Mathieu Rocaboy and Fr{\'e}d{\'e}ric Kerff and Paulette Charlier and Eric Sauvage and R F Pratt},
  journal={Biochemistry},
  year={2010},
  volume={49 30},
  pages={
          6411-9
        }
}
The Actinomadura R39 DD-peptidase is a bacterial low molecular weight class C penicillin-binding protein. It has previously been shown to catalyze hydrolysis and aminolysis of small D-alanyl-D-alanine terminating peptides, especially those with a side chain that mimics the amino terminus of the stem peptide precursor to the bacterial cell wall. This paper describes the synthesis of (D-alpha-aminopimelylamino)-D-1-ethylboronic acid, designed to be a peptidoglycan-mimetic transition state… CONTINUE READING
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