Entry |
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Name |
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Class |
Hydrolases;
Acting on peptide bonds (peptidases);
Serine endopeptidases
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Reaction(IUBMB) |
Cleaves -Ala!Ser- and -Ala!Ala- bonds in the scaffold protein
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Comment |
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
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History |
EC 3.4.21.97 created 2000
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Orthology |
K21078 | Betaherpesvirinae capsid scaffolding protein |
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Reference |
|
Authors |
Chen P, Tsuge H, Almassy RJ, Gribskov CL, Katoh S, Vanderpool DL, Margosiak SA, Pinko C, Matthews DA, Kan CC. |
Title |
Structure of the human cytomegalovirus protease catalytic domain reveals a novel serine protease fold and catalytic triad. |
Journal |
|
Reference |
2 |
Authors |
Darke, P.L. |
Title |
Herpesvirus assemblin. |
Journal |
In: Barrett, A.J., Rawlings, N.D. and Woessner, J.F. (Eds.), Handbook of Proteolytic Enzymes, Academic Press, London, 1998, p. 470-472. |
Other DBs |
ExPASy - ENZYME nomenclature database: | 3.4.21.97 |
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