Peptidase Do
| Peptidase Do | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| 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
- ^ 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.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ 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.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ 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.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ 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.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ 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.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ 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.
{{cite journal}}: CS1 maint: multiple names: authors list (link)
External links
- Peptidase+Do at the U.S. National Library of Medicine Medical Subject Headings (MeSH)