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The catalytic mechanism of DD-peptidases: unexpected importance of tyrosine 280 in the transpeptidation reaction catalysed by the Streptomyces R61 DD-peptidase

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Abstract.

The study of the interactions between the Tyr280Phe mutant of the Streptomyces R61 DD-peptidase, various substrates and β-lactam antibiotics shows that Tyr280 is involved not only in the formation of the acylenzyme with the peptide substrate and β-lactam antibiotics, but also and specifically in the catalysis of the transpeptidation reaction. Surprisingly, this residue does not belong to the conserved structural and functional elements which characterise the penicillin-recognising enzymes.

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Authors and Affiliations

  1. Centre d'Ingénierie des Protéines et Laboratoire d'Enzymologie, Université de Liège, Institut de Chimie B6, Sart-Tilman, B-4000 Liège (Belgium), Fax +32 43 66 33 64, e-mail: jmfrere@ulg.ac.be, , , , , , BE

    J.-M. Wilkin, J. Lamotte-Brasseur & J.-M. Frère

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  1. J.-M. Wilkin
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  2. J. Lamotte-Brasseur
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  3. J.-M. Frère
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Received 30 April 1998; accepted 5 May 1998

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Wilkin, JM., Lamotte-Brasseur, J. & Frère, JM. The catalytic mechanism of DD-peptidases: unexpected importance of tyrosine 280 in the transpeptidation reaction catalysed by the Streptomyces R61 DD-peptidase. CMLS, Cell. Mol. Life Sci. 54, 726–732 (1998). https://doi.org/10.1007/s000180050200

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  • DOI: https://doi.org/10.1007/s000180050200

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