Requirement of lid2 for interfacial activation of a family I.3 lipase with unique two lid structures.

@article{Cheng2012RequirementOL,
  title={Requirement of lid2 for interfacial activation of a family I.3 lipase with unique two lid structures.},
  author={Maria Cheng and Clement Angkawidjaja and Yuichi Koga and Shigenori Kanaya},
  journal={The FEBS journal},
  year={2012},
  volume={279 19},
  pages={3727-3737}
}
A family I.3 lipase from Pseudomonas sp. MIS38 (PML) is characterized by the presence of two lids (lid1 and lid2) that greatly change conformation upon substrate binding. While lid1 represents the commonly known lid in lipases, lid2 is unique to PML and other family I.3 lipases. To clarify the role of lid2 in PML, a lid2 deletion mutant (ΔL2-PML) was constructed by deleting residues 35-64 of PML. ΔL2-PML requires calcium ions for both lipase and esterase activities as does PML, suggesting that… CONTINUE READING
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