Peptidase Do

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. 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, 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

Peptidase+Do at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

v t e Endopeptidases: serine proteases/serine endopeptidases (EC 3.4.21)
Digestive enzymes	Enteropeptidase Trypsin Chymotrypsin Elastase Neutrophil Pancreatic
Coagulation	factors: Thrombin Factor VIIa Factor IXa Factor Xa Factor XIa Factor XIIa Kallikrein PSA KLK1 KLK2 KLK3 KLK4 KLK5 KLK6 KLK7 KLK8 KLK9 KLK10 KLK11 KLK12 KLK13 KLK14 KLK15 fibrinolysis: Plasmin Plasminogen activator Tissue plasminogen activator Urinary plasminogen activator
Complement system	Factor B Factor D Factor I MASP MASP1 MASP2 C3-convertase
Other immune system	Chymase Granzyme Tryptase Proteinase 3/Myeloblastin
Venombin	Ancrod Batroxobin
Other	Acrosin Prolyl endopeptidase Pronase Proprotein convertases 1 2 Prostasin Reelin Subtilisin/Furin/S1P4 Sedolisin/TPP1 Streptokinase Cathepsin A G

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

Portal:

Biology

Category:

EC 3.4.21