Reaction: Hydrolysis of an asparaginyl bond involved in the maturation of the structural protein of the virus, typically -AsnAla- or -AsnPhe-
Other names: Black Beetle virus endopeptidase; Flock House virus endopeptidase
Comments: A single aspartic residue is critical for activity, and inhibition by EDTA indicates that a metal ion is also important. The enzyme is known from several nodaviruses that are pathogens of insects. Type example of peptidase family A6, and structurally related to the tetravirus endopeptidase in family A21, although in that family, the catalytic residue is thought to be Glu.
Links to other databases: BRENDA, EXPASY, KEGG, MEROPS, Metacyc, PDB, CAS registry number: 852954-38-2
1. Zlotnick, A., Reddy, V.S., Dasgupta, R., Schneemann, A., Ray,W.J., Jr., Rueckert, R.R. and Johnson, J.E. Capsid assembly in a family of animal viruses primes an autoproteolytic maturation that depends on a single aspartic acid residue. J. Biol. Chem. 269 (1994) 13680-13684. [PMID: 8175803]
2. Johnson, J.E. and Schneemann, A. Nodavirus endopeptidase. In: Barrett, A.J., Rawlings, N.D. and Woessner, J.F. (Eds.), Handbook of Proteolytic Enzymes, Academic Press, London, 1998, pp. 964-967.