Peptidase Do

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Peptidase Do
Protease do homo24mer, E.Coli
EC number
CAS number 161108-11-8
IntEnz IntEnz view
ExPASy NiceZyme view
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

Peptidase Do (EC, 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.


  1. ^ Lipinska, B.; Zylicz, M.; Georgopoulos, C. (1990). "The HtrA (DegP) protein, essential for Escherichia coli survival at high temperatures, is an endopeptidase". J. Bacteriol. 172 (4): 1791–1797. PMC 208670Freely accessible. PMID 2180903. doi:10.1128/jb.172.4.1791-1797.1990. 
  2. ^ Seol, J.H.; Woo, S.K.; Jung, E.M.; Yoo, S.J.; Lee, C.S.; Kim, K.J.; Tanaka, K.; Ichihara, A.; Ha, D.B.; Chung, C.H. (1991). "Protease Do is essential for survival of Escherichia coli at high temperatures: its identity with the htrA gene product". Biochem. Biophys. Res. Commun. 176 (2): 730–736. PMID 2025286. doi:10.1016/s0006-291x(05)80245-1. 
  3. ^ Jones, C.H.; Dexter, P.; Evans, A.K.; Liu, C.; Hultgren, S.J.; Hruby, D.E. (2002). "Escherichia coli DegP protease cleaves between paired hydrophobic residues in a natural substrate: the PapA pilin". J. Bacteriol. 184 (20): 5762–5771. PMC 139609Freely accessible. PMID 12270835. doi:10.1128/jb.184.20.5762-5771.2002. 
  4. ^ Swamy, K.H.; Chung, C.H.; Goldberg, A.L. (1983). "Isolation and characterization of protease Do from Escherichia coli, a large serine protease containing multiple subunits". Arch. Biochem. Biophys. 224 (2): 543–554. PMID 6347072. doi:10.1016/0003-9861(83)90242-4. 
  5. ^ Pallen, M.J.; Wren, B.W. (1997). "The HtrA family of serine proteases". Mol. Microbiol. 26 (2): 209–221. PMID 9383148. doi:10.1046/j.1365-2958.1997.5601928.x. 
  6. ^ Krojer, T.; Garrido-Franco, M.; Huber, R.; Ehrmann, M.; Clausen, T. (2002). "Crystal structure of DegP (HtrA) reveals a new protease-chaperone machine". Nature. 416: 455–459. PMID 11919638. doi:10.1038/416455a. 

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