• Corpus ID: 982738

Studying enzyme-beta-lactam interactions using X-ray diffraction.

@article{Kelly1989StudyingEI,
  title={Studying enzyme-beta-lactam interactions using X-ray diffraction.},
  author={Judith A. Kelly and James R. Knox and H. Zhao},
  journal={Journal of molecular graphics},
  year={1989},
  volume={7 2},
  pages={
          87-92
        }
}

• J. A. Kelly, J. Knox, H. Zhao
• Published 1989
• Chemistry, Biology
• Journal of molecular graphics

The interaction of representative beta-lactam antibiotics with a bacterial enzyme target has been mapped in three dimensions using X-ray diffraction data to 2.25 A resolution. Examination of complexes of cephalosporin C, benzylmonobactam, and alpha-(2,3)-methylenepenicillin G with the D-alanyl-D-alanine transpeptidase-carboxypeptidase from Streptomyces R61 shows that the enzyme's reactive serine has acylated the beta-lactam ring of each inhibitor. The known half-lives of the three acyl complexes can be correlated with the distance of the drug's carboxylate (or sulfonate) group from complementary groups on the DD-peptidase.