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l-aspartyl and l-asparaginyl residues in proteins spontaneously undergo intra-residue rearrangements forming isoaspartyl/β-aspartyl residues linked through their side-chain β-carboxyl group with the following amino acid. In order to avoid accumulation of isoaspartyl dipeptides left over from protein degradation, some bacteria have developed specialized isoaspartyl/β-aspartyl zinc dipeptidases sequentially...
PepV from Lactobacillus delbrueckii, a dinuclear zinc peptidase, has been characterized as an unspecific amino dipeptidase. The crystal structure of PepV in complex with the phosphinic inhibitor AspΨ[PO 2 CH 2 ]AlaOH, a dipeptide substrate mimetic, reveals a ''catalytic domain'' and a ''lid domain,'' which together form an internal active site cavity that traps the inhibitor. The catalytic...
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