Biology:Peptidase Do

From HandWiki

Peptidase Do (EC 3.4.21.107, DegP, DegP protease, HtrA, high temperature requirement protease A, HrtA heat shock protein, protease Do, Do protease) is an enzyme.[1][2][3][4][5][6] This enzyme catalyses the following chemical reaction

Acts on substrates that are at least partially unfolded. The cleavage site P1 residue is normally between a pair of hydrophobic residues, such as Val-Val

This Escherichia coli serine endopeptidase is essential for the clearance of denatured proteins from the inner-membrane and periplasmic space.

References

  1. "The HtrA (DegP) protein, essential for Escherichia coli survival at high temperatures, is an endopeptidase". Journal of Bacteriology 172 (4): 1791–7. April 1990. doi:10.1128/jb.172.4.1791-1797.1990. PMID 2180903. 
  2. "Protease Do is essential for survival of Escherichia coli at high temperatures: its identity with the htrA gene product". Biochemical and Biophysical Research Communications 176 (2): 730–6. April 1991. doi:10.1016/s0006-291x(05)80245-1. PMID 2025286. 
  3. "Escherichia coli DegP protease cleaves between paired hydrophobic residues in a natural substrate: the PapA pilin". Journal of Bacteriology 184 (20): 5762–71. October 2002. doi:10.1128/jb.184.20.5762-5771.2002. PMID 12270835. 
  4. "Isolation and characterization of protease do from Escherichia coli, a large serine protease containing multiple subunits". Archives of Biochemistry and Biophysics 224 (2): 543–54. July 1983. doi:10.1016/0003-9861(83)90242-4. PMID 6347072. 
  5. "The HtrA family of serine proteases". Molecular Microbiology 26 (2): 209–21. October 1997. doi:10.1046/j.1365-2958.1997.5601928.x. PMID 9383148. 
  6. "Crystal structure of DegP (HtrA) reveals a new protease-chaperone machine". Nature 416 (6879): 455–9. March 2002. doi:10.1038/416455a. PMID 11919638. 

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