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Nitanai, Y. et al.

Nitanai, Satow, Adachi, Tsujimoto,

Crystal structure of human renal dipeptidase involved in beta-lactam hydrolysis.

Human renal dipeptidase is a membrane-bound glycoprotein hydrolyzing dipeptides and is involved in hydrolytic metabolism of penem and carbapenem beta-lactam antibiotics. The crystal structures of the saccharide-trimmed enzyme are determined as unliganded and inhibitor-liganded forms. They are informative for designing new antibiotics that are not hydrolyzed by this enzyme. The active site in each of the (alpha/beta)(8) barrel subunits of the homodimeric molecule is composed of binuclear zinc ions bridged by the Glu125 side-chain located at the bottom of the barrel, and it faces toward the microvillar membrane of a kidney tubule. A dipeptidyl moiety of the therapeutically used cilastatin inhibitor is fully accommodated in the active-site pocket, which is small enough for precise recognition of dipeptide substrates. The barrel and active-site architectures utilizing catalytic metal ions exhibit unexpected similarities to those of the murine adenosine deaminase and the catalytic domain of the bacterial urease.[1]

References

Crystal structure of human renal dipeptidase involved in beta-lactam hydrolysis. Nitanai, Y., Satow, Y., Adachi, H., Tsujimoto, M. J. Mol. Biol. (2002) [Pubmed]

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