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

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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