HtrA2 peptidase

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

↑ Srinivasula, S.M., Gupta, S., Datta, P., Zhang, Z., Hegde, R., Cheong, N., Fernandes-Alnemri, T. and Alnemri, E.S. (2003). "Inhibitor of apoptosis proteins are substrates for the mitochondrial serine protease Omi/HtrA2". J. Biol. Chem. 278: 31469–31472. doi:10.1074/jbc.C300240200. PMID 12835328.
↑ Savopoulos, J.W., Carter, P.S., Turconi, S., Pettman, G.R., Karran, E.H., Gray, C.W., Ward, R.V., Jenkins, O. and Creasy, C.L. (2000). "Expression, purification, and functional analysis of the human serine protease HtrA2". Protein. Expr. Purif. 19: 227–234. doi:10.1006/prep.2000.1240. PMID 10873535.
↑ Martins, L.M., Turk, B.E., Cowling, V., Borg, A., Jarrell, E.T., Cantley, L.C. and Downward, J. (2003). "Binding specificity and regulation of the serine protease and PDZ domains of HtrA2/Omi". J. Biol. Chem. 278 (49): 49417–49427. doi:10.1074/jbc.M308659200. PMID 14512424.
↑ Gray, C.W., Ward, R.V., Karran, E., Turconi, S., Rowles, A., Viglienghi, D., Southan, C., Barton, A., Fantom, K.G., West, A., Savopoulos, J., Hassan, N.J., Clinkenbeard, H., Hanning, C., Amegadzie, B., Davis, J.B., Dingwall, C., Livi, G.P. and Creasy, C.L. (2000). "Characterization of human HtrA2, a novel serine protease involved in the mammalian cellular stress response". Eur. J. Biochem. 267: 5699–5710. doi:10.1046/j.1432-1327.2000.01589.x. PMID 10971580.
↑ Li, W., Srinivasula, S.M., Chai, J., Li, P., Wu, J.W., Zhang, Z., Alnemri, E.S. and Shi, Y. (2002). "Structural insights into the pro-apoptotic function of mitochondrial serine protease HtrA2/Omi". Nat. Struct. Biol. 9 (6): 436–441. doi:10.1038/nsb795. PMID 11967569.

External links

HtrA2 peptidase 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

Proteins: 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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