Structure of malonamidase E2 reveals a novel Ser-cisSer-Lys catalytic triad in a new serine hydrolase fold that is prevalent in nature.

@article{Shin2002StructureOM,
  title={Structure of malonamidase E2 reveals a novel Ser-cisSer-Lys catalytic triad in a new serine hydrolase fold that is prevalent in nature.},
  author={Sejeong Shin and Tae-Hee Lee and Nam-Chul Ha and Hyun Min Koo and So-Yeon Kim and H Lee and Yu Sam Kim and Byung-Ha Oh},
  journal={The EMBO journal},
  year={2002},
  volume={21 11},
  pages={
          2509-16
        }
}
A large group of hydrolytic enzymes, which contain a conserved stretch of approximately 130 amino acids designated the amidase signature (AS) sequence, constitutes a super family that is distinct from any other known hydrolase family. AS family enzymes are widespread in nature, ranging from bacteria to humans, and exhibit a variety of biological functions. Here we report the first structure of an AS family enzyme provided by the crystal structure of malonamidase E2 from Bradyrhizobium japonicum… CONTINUE READING
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