HtrA2 peptidase (EC 3.4.21.108, high temperature requirement protein A2, HtrA2, Omi stress-regulated endoprotease, serine proteinase OMI, OMI/HtrA2 protease, HtrA2/Omi, Omi/HtrA2) is an enzyme.^[1]^[2]^[3]^[4]^[5] This enzyme catalyses the following chemical reaction

Cleavage of non-polar aliphatic amino-acids at the P1 position, with a preference for Val, Ile and Met.

This enzyme is upregulated in mammalian cells in response to stress induced by heat shock and tunicamycin treatment.

References[edit]

^ Srinivasula SM, Gupta S, Datta P, Zhang Z, Hegde R, Cheong N, Fernandes-Alnemri T, Alnemri ES (August 2003). "Inhibitor of apoptosis proteins are substrates for the mitochondrial serine protease Omi/HtrA2". The Journal of Biological Chemistry. 278 (34): 31469–72. doi:10.1074/jbc.C300240200. PMID 12835328.

^ Savopoulos JW, Carter PS, Turconi S, Pettman GR, Karran EH, Gray CW, Ward RV, Jenkins O, Creasy CL (July 2000). "Expression, purification, and functional analysis of the human serine protease HtrA2". Protein Expression and Purification. 19 (2): 227–34. doi:10.1006/prep.2000.1240. PMID 10873535.

^ Martins LM, Turk BE, Cowling V, Borg A, Jarrell ET, Cantley LC, Downward J (December 2003). "Binding specificity and regulation of the serine protease and PDZ domains of HtrA2/Omi". The Journal of Biological Chemistry. 278 (49): 49417–27. doi:10.1074/jbc.M308659200. PMID 14512424.

^ Gray CW, Ward RV, Karran E, Turconi S, Rowles A, Viglienghi D, Southan C, Barton A, Fantom KG, West A, Savopoulos J, Hassan NJ, Clinkenbeard H, Hanning C, Amegadzie B, Davis JB, Dingwall C, Livi GP, Creasy CL (September 2000). "Characterization of human HtrA2, a novel serine protease involved in the mammalian cellular stress response". European Journal of Biochemistry. 267 (18): 5699–710. doi:10.1046/j.1432-1327.2000.01589.x. PMID 10971580.

^ Li W, Srinivasula SM, Chai J, Li P, Wu JW, Zhang Z, Alnemri ES, Shi Y (June 2002). "Structural insights into the pro-apoptotic function of mitochondrial serine protease HtrA2/Omi". Nature Structural Biology. 9 (6): 436–41. doi:10.1038/nsb795. PMID 11967569.

External links[edit]

HtrA2+peptidase 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)

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