Thiol dioxygenases: unique families of cupin proteins

@article{Stipanuk2010ThiolDU,
  title={Thiol dioxygenases: unique families of cupin proteins},
  author={Martha H. Stipanuk and Chad R Simmons and P. Andrew Karplus and John E. Dominy},
  journal={Amino Acids},
  year={2010},
  volume={41},
  pages={91-102}
}
Proteins in the cupin superfamily have a wide range of biological functions in archaea, bacteria and eukaryotes. Although proteins in the cupin superfamily show very low overall sequence similarity, they all contain two short but partially conserved cupin sequence motifs separated by a less conserved intermotif region that varies both in length and amino acid sequence. Furthermore, these proteins all share a common architecture described as a six-stranded β-barrel core, and this canonical cupin… CONTINUE READING

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References

Publications referenced by this paper.
Showing 1-10 of 47 references

An Febound persulfenate intermediate in cysteine dioxyenase

CR Simmons, K Krishnamoorthy, +5 authors PA Karplus
Biochemistry • 2008
View 6 Excerpts
Highly Influenced

Structure and mechanism of mouse cysteine dioxygenase.

Proceedings of the National Academy of Sciences of the United States of America • 2006
View 9 Excerpts
Highly Influenced

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