EC 3.4.22.44 - Nuclear-inclusion-a endopeptidase

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IntEnz Enzyme Nomenclature
EC 3.4.22.44

Names

Accepted name:
nuclear-inclusion-a endopeptidase
Other name:
potyvirus NIa protease
Systematic name:

Reaction

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

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , MEROPS , UniPathway
Structural data: CSA , EC2PDB
UniProtKB/Swiss-Prot: (38) [show] [UniProt]

References

  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: 1309-1319 (1998).
  2. Kim, D.-H. and Choi, K.Y.
    Potyvirus NIa protease.
    In: Barrett, A.J., Rawlings, N.D. and Woessner, J.F. (Eds.) Handbook of Proteolytic Enzymes, Academic Press, London, 1998, 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: 953-958 (1998). [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: 183-190 (1996). [PMID: 8955037]

[EC 3.4.22.44 created 2000]