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Peptidase activity of beta-lactamases

Rhazi, N ; Galleni, M ; Page, M I ; Frère, J M

Biochemical journal, 1999-07, Vol.341 ( Pt 2) (2), p.409-413 [Periódico revisado por pares]

England: Portland Press

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  • Título:
    Peptidase activity of beta-lactamases
  • Autor: Rhazi, N ; Galleni, M ; Page, M I ; Frère, J M
  • Assuntos: Bacillus - enzymology ; beta-Lactamases - chemistry ; beta-Lactamases - metabolism ; Carboxypeptidases - chemistry ; Carboxypeptidases - metabolism ; Catalysis ; Catalytic mechanism ; DD-peptidases ; Hydrolysis ; kinetics ; Life sciences ; Microbiologie ; Microbiology ; Sciences du vivant ; Substrate Specificity
  • É parte de: Biochemical journal, 1999-07, Vol.341 ( Pt 2) (2), p.409-413
  • Notas: ObjectType-Article-1
    SourceType-Scholarly Journals-1
    ObjectType-Feature-2
    content type line 23
    scopus-id:2-s2.0-0033565411
  • Descrição: Although beta-lactamases have generally been considered as being devoid of peptidase activity, a low but significant hydrolysis of various N-acylated dipeptides was observed with representatives of each class of beta-lactamases. The kcat/Km values were below 0.1 M(-1). s(-1), but the enzyme rate enhancement factors were in the range 5000-20000 for the best substrates. Not unexpectedly, the best 'peptidase' was the class C beta-lactamase of Enterobacter cloacae P99, but, more surprisingly, the activity was always higher with the phenylacetyl- and benzoyl-d-Ala-d-Ala dipeptides than with the diacetyl- and alpha-acetyl-l-Lys-d-Ala-d-Ala tripeptides, which are the preferred substrates of the low-molecular-mass, soluble dd-peptidases. A comparison between the beta-lactamases and dd-peptidases showed that it might be as difficult for a dd-peptidase to open the beta-lactam ring as it is for the beta-lactamases to hydrolyse the peptides, an observation which can be explained by geometric and stereoelectronic considerations.
  • Editor: England: Portland Press
  • Idioma: Inglês
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  • Realização: ABCD-USP USP   Logos de Redes Sociais: Freepik

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