Critical involvement of a carbamylated lysine in catalytic function of class D beta-lactamases.

@article{Golemi2001CriticalIO,
  title={Critical involvement of a carbamylated lysine in catalytic function of class D beta-lactamases.},
  author={Dasantila Golemi and Laurent Maveyraud and Sergei Vakulenko and Jean Samama and Shahriar Mobashery},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2001},
  volume={98 25},
  pages={14280-5}
}
beta-Lactamases are the resistance enzymes for beta-lactam antibiotics, of which four classes are known. beta-lactamases hydrolyze the beta-lactam moieties of these antibiotics, rendering them inactive. It is shown herein that the class D OXA-10 beta-lactamase depends critically on an unusual carbamylated lysine as the basic residue for both the enzyme acylation and deacylation steps of catalysis. The formation of carbamylated lysine is reversible. Evidence is presented that this enzyme is… CONTINUE READING