ExplorEnz: EC 3.4.21.97

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3.4.21.97

Accepted name:

assemblin

Reaction:

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

Comments:

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

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 139691-88-6

References:

1.	Chen, P., Tsuge, H., Almassy, R.J., Gribskov, C.L., Katoh, S., Vanderpool, D.L., Margosiak, S.A., Pinko, C., Matthews, D.A. and Kan, C.C. Structure of the human cytomegalovirus protease catalytic domain reveals a novel serine protease fold and catalytic triad. Cell 86 (1996) 477–483. [DOI] [PMID: 8797829]
2.	Darke, P.L. Herpesvirus assemblin. In: Barrett, A.J., Rawlings, N.D. and Woessner, J.F. (Ed.), Handbook of Proteolytic Enzymes, Academic Press, London, 1998, pp. 470–472.

[EC 3.4.21.97 created 2000]