EC Number |
Natural Substrates |
---|
3.4.22.44 | amyloid-beta + H2O |
- |
3.4.22.44 | more |
interaction between purified recombinant NIa-Pro and VPg domains, overview |
3.4.22.44 | more |
the enzyme interacts with proteins EIF3G, FBPA1, FK506BP, GTPBP, MSRB1, and MTL |
3.4.22.44 | nuclear inclusion protein a + H2O |
- |
3.4.22.44 | nuclear inclusion protein a + H2O |
identification of cleavage site |
3.4.22.44 | nuclear inclusion protein a + H2O |
analysis of cleavage sites, specific for its own polypeptide chain, no cleavage of other potyvirus NIa proteins |
3.4.22.44 | nuclear inclusion protein a + H2O |
the nuclear inclusion protein of potyviruses has two domains, the Vpg domain of 22 kDa and the C-terminal domain of 27 kDa which has proteolytic activity. The first cleavage at Ser223-Gly224 produces a 25 kDa protein. TuMV cleaves itself in cis, removing a 20 amino aicd peptide from the C-terminus. A second cleavage is very slow and occurs between Thr207-Ser208, resulting in a 24 kDa protein |
3.4.22.44 | P-sG polyprotein + H2O |
- |