Peptidase Do
| Peptidase Do | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Protease do homo24mer, E.Coli | |||||||||
| Identifiers | |||||||||
| EC no. | 3.4.21.107 | ||||||||
| CAS no. | 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
[edit]- ^ Lipinska B, Zylicz M, Georgopoulos C (April 1990). "The HtrA (DegP) protein, essential for Escherichia coli survival at high temperatures, is an endopeptidase". Journal of Bacteriology. 172 (4): 1791–7. doi:10.1128/jb.172.4.1791-1797.1990. PMC 208670. PMID 2180903.
- ^ Seol JH, Woo SK, Jung EM, Yoo SJ, Lee CS, Kim KJ, Tanaka K, Ichihara A, Ha DB, Chung CH (April 1991). "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. doi:10.1016/s0006-291x(05)80245-1. PMID 2025286.
- ^ Jones CH, Dexter P, Evans AK, Liu C, Hultgren SJ, Hruby DE (October 2002). "Escherichia coli DegP protease cleaves between paired hydrophobic residues in a natural substrate: the PapA pilin". Journal of Bacteriology. 184 (20): 5762–71. doi:10.1128/jb.184.20.5762-5771.2002. PMC 139609. PMID 12270835.
- ^ Swamy KH, Chung CH, Goldberg AL (July 1983). "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. doi:10.1016/0003-9861(83)90242-4. PMID 6347072.
- ^ Pallen MJ, Wren BW (October 1997). "The HtrA family of serine proteases". Molecular Microbiology. 26 (2): 209–21. doi:10.1046/j.1365-2958.1997.5601928.x. PMID 9383148.
- ^ Krojer T, Garrido-Franco M, Huber R, Ehrmann M, Clausen T (March 2002). "Crystal structure of DegP (HtrA) reveals a new protease-chaperone machine". Nature. 416 (6879): 455–9. doi:10.1038/416455a. PMID 11919638.
External links
[edit]- Peptidase+Do at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
