Peptidase Do

Peptidase Do
Identifiers
EC number 3.4.21.107
CAS number 161108-11-8
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB 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. ↑ Lipinska, B., Zylicz, M. and Georgopoulos, C. (1990). "The HtrA (DegP) protein, essential for Escherichia coli survival at high temperatures, is an endopeptidase". J. Bacteriol. 172 (4): 1791–1797. PMID 2180903.
  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. and 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. doi:10.1016/s0006-291x(05)80245-1. PMID 2025286.
  3. ↑ Jones, C.H., Dexter, P., Evans, A.K., Liu, C., Hultgren, S.J. and 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. doi:10.1128/jb.184.20.5762-5771.2002. PMID 12270835.
  4. ↑ Swamy, K.H., Chung, C.H. and 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. doi:10.1016/0003-9861(83)90242-4. PMID 6347072.
  5. ↑ Pallen, M.J. and Wren, B.W. (1997). "The HtrA family of serine proteases". Mol. Microbiol. 26 (2): 209–221. doi:10.1046/j.1365-2958.1997.5601928.x. PMID 9383148.
  6. ↑ Krojer, T., Garrido-Franco, M., Huber, R., Ehrmann, M. and Clausen, T. (2002). "Crystal structure of DegP (HtrA) reveals a new protease-chaperone machine". Nature 416: 455–459. doi:10.1038/416455a. PMID 11919638.

External links

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