The Enzyme Database

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Accepted name: nuclear-inclusion-a endopeptidase
Reaction: Hydrolyses glutaminyl bonds, and activity is further restricted by preferences for the amino acids in P6 - P1′ that vary with the species of potyvirus, e.g. Glu-Xaa-Xaa-Tyr-Xaa-Gln┼(Ser or Gly) for the enzyme from tobacco etch virus. The natural substrate is the viral polyprotein, but other proteins and oligopeptides containing the appropriate consensus sequence are also cleaved.
Other name(s): potyvirus NIa protease
Comments: The potyviruses cause diseases in plants, and inclusion bodies appear in the host cell nuclei; protein a of the inclusion bodies is the endopeptidase. The enzyme finds practical use when encoded in vectors for the artificial expression of recombinant fusion proteins, since it can confer on them the capacity for autolytic cleavage. It is also reported that transgenic plants expressing the enzyme are resistant to viral infection. Type example of peptidase family C4.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 139946-51-3
1.  Fellers, J.P., Collins, G.B. and Hunt, A.G. The NIa-proteinase of different plant potyviruses provides specific resistance to viral infection. Crop Sci. 38 (1998) 1309–1319.
2.  Kim, D.-H. and Choi, K.Y. Potyvirus NIa protease. In: Barrett, A.J., Rawlings, N.D. and Woessner, J.F. (Ed.), Handbook of Proteolytic Enzymes, Academic Press, London, 1998, pp. 721–723.
3.  Takahashi, T., Nakanishi, M., Yao, Y., Uyeda, I. and Serizawa, N. Direct formation of human interleukin-11 by cis-acting system of plant virus protease in Escherichia coli. Biosci. Biotechnol. Biochem. 62 (1998) 953–958. [PMID: 9648226]
4.  Kim, D.H., Hwang, D.C., Kang, B.H., Lew, J., Han, J.S., Song, B.O.D. and Choi, K.Y. Effects of internal cleavages and mutations in the C-terminal region of NIa protease of turnip mosaic potyvirus on the catalytic activity. Virology 226 (1996) 183–190. [DOI] [PMID: 8955037]
[EC created 2000]

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