Biochemical Journal 1986-04-01

Streptomyces K15 DD-peptidase-catalysed reactions with suicide beta-lactam carbonyl donors.

M Leyh-Bouille, M Nguyen-Distèche, S Pirlot, A Veithen, C Bourguignon, J M Ghuysen

Index: Biochem. J. 235(1) , 177-82, (1986)

Full Text: HTML

Abstract

The values of the kinetic parameters that govern the interactions between the Streptomyces K15 DD-peptidase and beta-lactam compounds were determined by measuring the inactivating effect that these compounds exert on the transpeptidase activity of the enzyme and, in the case of [14C]benzylpenicillin and [14C]cefoxitin, by measuring the amounts of acyl-enzyme formed during the reaction. K15 DD-peptidase binds benzylpenicillin or cefoxitin at a molar ratio of 1:1. Benzylpenicilloate is the major product released during breakdown of the acyl-enzyme formed with benzylpenicillin. Benzylpenicillin is not a better acylating agent than the amide Ac2-L-Lys-D-Ala-D-Ala and ester Ac2-L-Lys-D-Ala-D-lactatecarbonyl-donor substrates. beta-Lactam compounds possessing a methoxy group on the alpha-face of the molecule show high inactivating potency.

Related Compounds

  • Ac-Lys(Ac)-D-Ala...

Related Articles:

Conformational studies of resin-bound vancomycin and the complex of vancomycin and Ac2-L-Lys-D-Ala-D-Ala.

2005-01-01

[J. Comb. Chem. 7(1) , 123-9, (2005)]

Isolation of the membrane-bound 26 000-Mr penicillin-binding protein of Streptomyces strain K15 in the form of a penicillin-sensitive D-alanyl-D-alanine-cleaving transpeptidase.

1982-10-01

[Biochem. J. 207 , 109, (1982)]

Conformational analysis of peptide substrates and inhibitors of the Zn2+ G and serine R61 D-alanyl-D-alanine peptidases.

1981-12-01

[Eur. J. Biochem. 121(1) , 221-32, (1981)]

Partitioning the loss in vancomycin binding affinity for D-Ala-D-Lac into lost H-bond and repulsive lone pair contributions.

2003-08-06

[J. Am. Chem. Soc. 125(31) , 9314-5, (2003)]

Preparation of biologically active ristocetin derivatives: replacements of the 1'-amino group.

1985-09-01

[J. Med. Chem. 28(9) , 1371-5, (1985)]

More Articles...