Peptidase Do Explained
Peptidase Do |
Ec Number: | 3.4.21.107 |
Cas Number: | 161108-11-8 |
Width: | 270 |
Peptidase Do (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.
Notes and References
- Lipinska B, Zylicz M, Georgopoulos C . The HtrA (DegP) protein, essential for Escherichia coli survival at high temperatures, is an endopeptidase . Journal of Bacteriology . 172 . 4 . 1791–7 . April 1990 . 2180903 . 208670 . 10.1128/jb.172.4.1791-1797.1990 .
- Seol JH, Woo SK, Jung EM, Yoo SJ, Lee CS, Kim KJ, Tanaka K, Ichihara A, Ha DB, Chung CH . 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 . 2025286 . 10.1016/s0006-291x(05)80245-1 .
- Jones CH, Dexter P, Evans AK, Liu C, Hultgren SJ, Hruby DE . 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 . 12270835 . 139609 . 10.1128/jb.184.20.5762-5771.2002 .
- Swamy KH, Chung CH, Goldberg AL . 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 . 6347072 . 10.1016/0003-9861(83)90242-4 .
- Pallen MJ, Wren BW . The HtrA family of serine proteases . Molecular Microbiology . 26 . 2 . 209–21 . October 1997 . 9383148 . 10.1046/j.1365-2958.1997.5601928.x . free .
- Krojer T, Garrido-Franco M, Huber R, Ehrmann M, Clausen T . Crystal structure of DegP (HtrA) reveals a new protease-chaperone machine . Nature . 416 . 6879 . 455–9 . March 2002 . 11919638 . 10.1038/416455a .