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Literature DB >> 1747125

Accumulation of acyl-enzyme in DD-peptidase-catalysed reactions with analogues of peptide substrates.

M Jamin¹, M Adam, C Damblon, L Christiaens, J M Frère.

Abstract

Thioester substrates can be used to study the hydrolysis and transfer reactions catalysed by beta-lactamases and DD-peptidases. With the latter enzymes, accumulation of the acyl-enzyme can be detected directly. The efficiency of various amines as acceptor substrates was in excellent agreement with previous results obtained with peptide substrates of the DD-peptidases. The results indicated the presence of a specific binding site for the acceptor substrates. Although most of the results agreed well with a simple partition model, more elaborate hypotheses will be needed to account for all the data presented.

Entities: Chemical

Mesh：

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Year: 1991 PMID： 1747125 PMCID： PMC1130576 DOI： 10.1042/bj2800499

Source DB: PubMed Journal: Biochem J ISSN： 0264-6021 Impact factor: 3.857

17 in total

1. Kinetics of interaction between the exocellular DD-carboxypeptidase-transpeptidase from Streptomyces R61 and beta-lactam antibiotics. A choice of models.

Authors: J M Frère; J M Ghuysen; M Iwatsubo
Journal: Eur J Biochem Date: 1975-09-15

2. The diversity of the catalytic properties of class A beta-lactamases.

Authors: A Matagne; A M Misselyn-Bauduin; B Joris; T Erpicum; B Granier; J M Frère
Journal: Biochem J Date: 1990-01-01 Impact factor: 3.857

3. Mode of interaction between beta-lactam antibiotics and the exocellular DD-carboxypeptidase--transpeptidase from Streptomyces R39.

Authors: N Fuad; J M Frère; J M Ghuysen; C Duez; M Iwatsubo
Journal: Biochem J Date: 1976-06-01 Impact factor: 3.857

4. Enzymic mechanisms involving concomitant transfer and hydrolysis reactions.

Authors: J M Frère
Journal: Biochem J Date: 1973-11 Impact factor: 3.857

5. Penicillin-sensitive DD-carboxypeptidase from Streptomyces strain R 61.

Authors: M Leyh-Bouille; J Coyette; J M Ghuysen; J Idczak; H R Perkins; M Nieto
Journal: Biochemistry Date: 1971-05-25 Impact factor: 3.162

6. beta-Lactamase-catalyzed hydrolysis of acyclic depsipeptides and acyl transfer to specific amino acid acceptors.

Authors: R F Pratt; C P Govardhan
Journal: Proc Natl Acad Sci U S A Date: 1984-03 Impact factor: 11.205

7. Molecular weight, amino acid composition and physicochemical properties of the exocellular DD-carboxypeptidase-transpeptidase of Streptomyces R39.

Authors: J M Frère; R Moreno; J M Ghuysen
Journal: Biochem J Date: 1974-10 Impact factor: 3.857

8. Streptomyces DD-carboxypeptidases as transpeptidases. The specificity for amino compounds acting as carboxyl acceptors.

Authors: H R Perkins; M Nieto; J M Frére; M Leyh-Bouille; J M Ghuysen
Journal: Biochem J Date: 1973-04 Impact factor: 3.857

9. Kinetics of concomitant transfer and hydrolysis reactions catalysed by the exocellular DD-carboxypeptidase-transpeptidase of streptomyces R61.

Authors: J M Frère; J M Ghuysen; H R Perkins; M Nieto
Journal: Biochem J Date: 1973-11 Impact factor: 3.857

10. Fluorescence and circular dichroism studies on the Streptomyces R61 DD-carboxypeptidase-transpeptidase. Penicillin binding by the enzyme.

Authors: M Nieto; H R Perkins; J M Frère; J M Ghuysen
Journal: Biochem J Date: 1973-11 Impact factor: 3.857

21 in total

1. The ponA gene of Enterococcus faecalis JH2-2 codes for a low-affinity class A penicillin-binding protein.

Authors: Colette Duez; Séverine Hallut; Noureddine Rhazi; Séverine Hubert; Ana Amoroso; Fabrice Bouillenne; André Piette; Jacques Coyette
Journal: J Bacteriol Date: 2004-07 Impact factor: 3.490

2. An easy method for deriving steady-state rate equations.

Authors: S G Waley
Journal: Biochem J Date: 1992-09-01 Impact factor: 3.857

3. Importance of the two tryptophan residues in the Streptomyces R61 exocellular DD-peptidase.

Authors: C Bourguignon-Bellefroid; J M Wilkin; B Joris; R T Aplin; C Houssier; F G Prendergast; J Van Beeumen; J M Ghuysen; J M Frère
Journal: Biochem J Date: 1992-03-01 Impact factor: 3.857

4. The bimodular G57-V577 polypeptide chain of the class B penicillin-binding protein 3 of Escherichia coli catalyzes peptide bond formation from thiolesters and does not catalyze glycan chain polymerization from the lipid II intermediate.

Authors: M Adam; C Fraipont; N Rhazi; M Nguyen-Distèche; B Lakaye; J M Frère; B Devreese; J Van Beeumen; Y van Heijenoort; J van Heijenoort; J M Ghuysen
Journal: J Bacteriol Date: 1997-10 Impact factor: 3.490