Physarolisin

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Physarolisin (EC 3.4.21.103, Dictyostelium discoideum aspartic proteinase, Dictyostelium discoideum aspartic proteinase E, Physarum flavicomum aspartic proteinase, Physarum polycephalum acid proteinase, Physarum aspartic proteinase, physaropepsin) is an enzyme.^[1]^[2]^[3]^[4]^[5] This enzyme catalyses the following chemical reaction

Milk clotting activity. Preferential cleavage of Gly⁸-Ser in B chain of insulin most rapidly, followed by Leu¹¹!Val, Cys(SO₃H)¹⁹-Gly and Phe²⁴-Phe.

This enzyme belongs in peptidase family S53.

References

↑ Henney, H.R. and Tavana, G. (1982). "Purification and some properties of an intracellular acid (carboxyl) proteinase from differentiating haploid cells of Physarum flavicomum". Exp. Mycol. 6: 161–170. doi:10.1016/0147-5975(82)90090-1.
↑ Murakami-Murofushi, K., Hiratsuka, A. and Ohta, J. (1984). "A novel acid protease from haploid amoebae of Physarum polycephalum, and its changes during mating and subsequent differentiation into diploid plasmodia". Cell Struct. Funct. 9: 311–315. doi:10.1247/csf.9.311.
↑ North, M.J. and Whyte, A. (1984). "Purification and characterization of two acid proteinases from Dictyostelium discoideum". J. Gen. Microbiol. 130: 123–134. doi:10.1099/00221287-130-1-123.
↑ Wlodawer, A., Li, M., Gustchina, A., Oyama, H., Dunn, B.M. and Oda, K. (2003). "Structural and enzymatic properties of the sedolisin family of serine-carboxyl peptidases". Acta Biochim. Pol. 50: 81–102. PMID 12673349.
↑ Nishii, W., Ueki, T., Miyashita, R., Kojima, M., Kim, Y.T., Sasaki, N., Murakami-Murofushi, K. and Takahashi, K. (2003). "Structural and enzymatic characterization of physarolisin (formerly physaropepsin) proves that it is a unique serine-carboxyl proteinase". Biochem. Biophys. Res. Commun. 301: 1023–1029. doi:10.1016/s0006-291x(03)00083-4. PMID 12589815.

External links

Physarolisin 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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