Residues required for activity in Escherichia coli o-succinylbenzoate synthase (OSBS) are not conserved in all OSBS enzymes.

@article{Zhu2012ResiduesRF,
  title={Residues required for activity in Escherichia coli o-succinylbenzoate synthase (OSBS) are not conserved in all OSBS enzymes.},
  author={Wan Wen Zhu and Chenxi Wang and Jacob Jipp and Lance Ferguson and Stephanie Lucas and Michael A. Hicks and Margaret E Glasner},
  journal={Biochemistry},
  year={2012},
  volume={51 31},
  pages={6171-81}
}
Understanding how enzyme specificity evolves will provide guiding principles for protein engineering and function prediction. The o-succinylbenzoate synthase (OSBS) family is an excellent model system for elucidating these principles because it has many highly divergent amino acid sequences that are <20% identical, and some members have evolved a second function. The OSBS family belongs to the enolase superfamily, members of which use a set of conserved residues to catalyze a wide variety of… CONTINUE READING
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