Part:BBa_K4496000:Design

Optimized Jararhagin for Pichia Pastoris

Assembly Compatibility:

• 10
  COMPATIBLE WITH RFC[10]
• 12
  COMPATIBLE WITH RFC[12]
• 21
  COMPATIBLE WITH RFC[21]
• 23
  COMPATIBLE WITH RFC[23]
• 25
  COMPATIBLE WITH RFC[25]
• 1000
  COMPATIBLE WITH RFC[1000]

Design Notes

Using bioinformatics tools, the best DNA gene sequence corresponding to the mRNA of the original part (GenBank: X68251.1) was found. With this, the absence of signal peptide was checked and the sequence was optimized for synthesis using the yeast Pichia Pastoris.

Source

https://www.ncbi.nlm.nih.gov/nuccore/X68251.1/

References

M.J.I. Paine, H.P. Desmond, R.D.G. Theakston, J.M. Crampton Purification, cloning and molecular characterization of a high molecular weight hemorrhagic metalloprotease, jararhagin, from Bothrops jararaca venom. Insights into the disintegrin-like gene family J. Biol. Chem., 267 (1992), pp. 22869-22876.

BJARNASON, J. B.; FOX, J. W. Snake venom metalloendopeptidases: Reprolysins. Proteolytic Enzymes: Aspartic and Metallo Peptidases, p. 345–368, 1995.

W. Bode, F.X. Gomis-Ruth, W. Stockler Astacins, serralysins, snake venom and matrix metalloproteinases exhibit identical zinc-binding environments (HEXXHXXGXXH and Met-turn) and topologies and should be grouped into a common family, the ‘metzincins’ FEBS Lett., 331 (1993), pp. 134-140.