Abstract
A feature common to many proteases, including aspartic proteinases, is that they are synthesised as inactive zymogens, subsequently undergoing proteolytic processing to yield the active enzyme. This is a way of assuring the correct folding of the proteinase, regulating its activity during biosynthesis and avoiding unwanted proteolysis. Most aspartic proteinases have a conserved N-terminal pro-segment, which is later removed (1). In pepsinogen, the pro-segment is located over the active site cleft, stabilized by salt bridges that are disrupted at low pH (2). In cathepsin D, apart from the N-terminal pro-segment and a C-terminal dipeptide there is another sequence which is also removed, located within the protein (3). Removal of this 2–7 amino acid long sequence gives rise to the two chain active cathepsin D.
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References
G. Koelsch, M. Mares, P. Metcalf, M. Fusek, Multiple functions of pro-parts of aspartic proteinase zymogens. FEBS Lett. 343: 6 (1994).
M.N.G. James, A.R. Sielecki, Molecular structure of an aspartic proteinase zymogen, porcine pepsinogen, at 1.8 Å resolution. Nature 319: 33 (1986).
S. Yonezawa, T. Takahashi, X.J. Wang, R.N. Wong, J.A. Hartsuck, J. Tang, Structures at the proteolytic processing region of cathepsin D. J. Biol. Chem. 263: 16504 (1988).
J. Kervinen, K. Törmäkangas, P. Runeberg-Roos, K. Guruprasad, T. Blundell, T.H. Teeri, Structure and possible function of aspartic proteinases in barley and other plants. In “Aspartic Proteinases: Structure, Function, Biology and Biomedical Implications”. K. Takahashi, ed., p 241, Springer Science+Business Media New York (1995).
C. Faro, M. Ramalho-Santos, P. Veríssimo, J. Pissarra, C. Frazäo, J. Costa, X.-l. Lin, J. Tang, E. Pires, Structural and functional aspects of cardosins. In “Structure and Function of Aspartic Proteinases: Retroviral and Cellular Enzymes”, M.N.G. James, ed., p., Springer Science+Business Media New York (1997).
P. Veríssimo, C. Faro, A.J.G. Moir, Y. Lin, J. Tang, E. Pires, Purification, characterization and partial amino acid sequencing of two novel aspartic proteinases from fresh flowers of Cynara cardunculus. Eur. J. Biochem. 235: 762(1996).
C. Faro, P. Veríssimo, A.J.G. Moir, Y. Lin, J. Tang, E. Pires, Cardosin A and B, aspartic proteases from the flowers of cardoon. In “Aspartic Proteinases: Structure, Function, Biology and Biomedical Implications”, K. Takahashi, ed., p 241, Springer Science+Business Media New York (1995).
M. Ramalho-Santos, J. Pissarra, P. Veríssimo, S. Pereira, R. Salema, E. Pires, C.J. Faro, Cardosin A, an abundant aspartic proteinase, accumulates in protein storage vacuoles of the stigmatic papillae of Cynara cardunculus L. Planta (accepted for publication) (1997).
J. Sambrook, E.F. Fritsch, T. Maniatis, Molecular cloning: a laboratory manual, Second Ed., Cold Spring Harbour Laboratory Press, New York (1989).
P. Veríssimo, C. Esteves, C.J. Faro, E.V. Pires, The vegetable rennet of Cynara cardunculus contains two proteinases with chymosin and pepsin-like specificities. Biotech. Lett. 17: 621 (1995).
M. Ramalho-Santos, P. Veríssimo, C. Faro, E. Pires, Action on bovine αsl-casein of cardosins A and B, aspartic proteinases from the flowers of the cardoon Cynara cardunculus L.. Biochim. Biophys. Acta 1297: 83(1996).
S. Pereira, H. Carvalho, C. Sunkel, R. Salema, Immunocytolocalization of glutamine synthetase in meso-phyll and phloem of leaves of Solanum tuberosum L. Protoplasma 167: 66 (1992).
K. Guruprasad, K. Törmäkangas, J. Kervinen, T. Blundell, Comparative modelling of barley-grain aspartic proteinase: a structural rationale for observed hydrolytic specificity. FEBS Lett. 352: 131 (1994).
J.S. O’Brien, Y Kishimoto, Saposin proteins: structure, function, and role in human lysosomal storage disorders. FASEB J. 5: 301 (1991).
Y. Zhu, G.E. Conner, Intermolecular association of lysosomal protein precursors during biosynthesis. J. Biol. Chem. 269:3846(1994).
K. Nakamura, K. Matsuoka, Protein targeting to the vacuole in plant cells. Plant Physiol. 101:1 (1993).
S.Y. Bednarek, N.V. Raikhel, The barley lectin carboxyl-terminal propeptide is a vacuolar protein sorting determinant in plants. Plant Cell 3: 1195 (1991).
J.E. Dombrowski, M.R. Schroeder, S.Y. Bednarek, N.V. Raikhel, Determination of the functional elements within the vacuolar targeting signal of barley lectin. Plant Cell 5: 587 (1993).
P. Runeberg-Roos, J. Kervinen, V Kovaleva, N.V Raikhel, S. Gal, The aspartic proteinase of barley is a vacuolar enzyme that processes probarley lectin in vitro. Plant Physiol. 105: 321 (1994).
J.S. O’Brien, G.S. Carson, H.-C. Seo, M. Hiraiwa, Y. Kishimoto, Identification of prosaposin as a neurotrophic factor. Proc. Natl. Acad. Sei. USA 91: 9593 (1994).
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Ramalho-Santos, M., Pissarra, J., Pires, E., Faro, C. (1998). Cardosinogen A. In: James, M.N.G. (eds) Aspartic Proteinases. Advances in Experimental Medicine and Biology, vol 436. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-5373-1_35
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DOI: https://doi.org/10.1007/978-1-4615-5373-1_35
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