Biology:Peptidase Do

From HandWiki
Peptidase Do
3mh6.jpg
Protease do homo24mer, E.Coli
Identifiers
EC number3.4.21.107
CAS number161108-11-8
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum

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. 

External links