Role of the conserved amino acids of the 'SDN' loop (Ser130, Asp131 and Asn132) in a class A beta-lactamase studied by site-directed mutagenesis.

@article{Jacob1990RoleOT,
  title={Role of the conserved amino acids of the 'SDN' loop (Ser130, Asp131 and Asn132) in a class A beta-lactamase studied by site-directed mutagenesis.},
  author={Friedrich Jacob and Bernard Joris and Sophie Lepage and J. A. Maquet Dusart and Jean Marie Fr{\`e}re},
  journal={The Biochemical journal},
  year={1990},
  volume={271 2},
  pages={
          399-406
        }
}
Ser130, Asp131 and Asn132 ('SDN') are highly conserved residues in class A beta-lactamases forming one wall of the active-site cavity. All three residues of the SDN loop in Streptomyces albus G beta-lactamase were modified by site-directed mutagenesis. The mutant proteins were expressed in Streptomyces lividans, purified from culture supernatants and their kinetic parameters were determined for several substrates. Ser130 was substituted by Asn, Ala and Gly. The first modification yielded an… CONTINUE READING
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