assemblin

Hydrolases;
Acting on peptide bonds (peptidases);
Serine endopeptidases

Cleaves -Ala!Ser- and -Ala!Ala- bonds in the scaffold protein

Involved in the breakdown of the scaffold protein during the late stages of assembly of the herpes-virus virion. Inhibited by diisopropyl fluorophosphate. Type example of peptidase family S21. Catalytic residues are His, Ser, His, a combination not known for any other peptidase, and the protein fold also is unique. Known from herpes viruses of several types, cytomegalovirus, Epstein-Barr virus and human herpesvirus 3

1  [PMID:8797829]

Chen P, Tsuge H, Almassy RJ, Gribskov CL, Katoh S, Vanderpool DL, Margosiak SA, Pinko C, Matthews DA, Kan CC.

Structure of the human cytomegalovirus protease catalytic domain reveals a novel serine protease fold and catalytic triad.

Cell. 86 (1996) 835-43.

human cytomegalovirus

2

Darke, P.L.

Herpesvirus assemblin.

In: Barrett, A.J., Rawlings, N.D. and Woessner, J.F. (Eds.), Handbook of Proteolytic Enzymes, Academic Press, London, 1998, p. 470-472.