Mimicking enzyme evolution by generating new (betaalpha)8-barrels from (betaalpha)4-half-barrels.

@article{Hcker2004MimickingEE,
  title={Mimicking enzyme evolution by generating new (betaalpha)8-barrels from (betaalpha)4-half-barrels.},
  author={Birte H{\"o}cker and J{\"o}rg Claren and Reinhard Sterner},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2004},
  volume={101 47},
  pages={
          16448-53
        }
}
Gene duplication and fusion events that multiply and link functional protein domains are crucial mechanisms of enzyme evolution. The analysis of amino acid sequences and three-dimensional structures suggested that the (betaalpha)8-barrel, which is the most frequent fold among enzymes, has evolved by the duplication, fusion, and mixing of (betaalpha)4-half-barrel domains. Here, we mimicked this evolutionary strategy by generating in vitro (betaalpha)8-barrels from (betaalpha)4-half-barrels that… CONTINUE READING

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