Peptidase Do

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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.
↑ 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.
↑ 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.
↑ 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.
↑ 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.
↑ 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

Peptidase Do at the US National Library of Medicine Medical Subject Headings (MeSH)

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 Streptokinase S1P Cathepsin A G

Enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases(list) EC2 Transferases(list) EC3 Hydrolases(list) EC4 Lyases(list) EC5 Isomerases(list) EC6 Ligases(list)

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