Tunable, post-translational hydroxylation of collagen Domains in Escherichia coli.

@article{Pinkas2011TunablePH,
  title={Tunable, post-translational hydroxylation of collagen Domains in Escherichia coli.},
  author={Daniel M Pinkas and Sheng Ding and Ronald T. Raines and Annelise E. Barron},
  journal={ACS chemical biology},
  year={2011},
  volume={6 4},
  pages={320-4}
}
Prolyl 4-hydroxylases are ascorbate-dependent oxygenases that play key roles in a variety of eukaryotic biological processes including oxygen sensing, siRNA regulation, and collagen folding. They perform their functions by catalyzing the post-translational hydroxylation of specific proline residues on target proteins to form (2S,4R)-4-hydroxyproline. Thus far, the study of these post-translational modifications has been limited by the lack of a prokaryotic recombinant expression system for… CONTINUE READING

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