KEGG   ENZYME: 3.4.21.97
Entry
EC 3.4.21.97                Enzyme                                 
Name
assemblin
Class
Hydrolases;
Acting on peptide bonds (peptidases);
Serine endopeptidases
Reaction(IUBMB)
Cleaves -Ala!Ser- and -Ala!Ala- bonds in the scaffold protein
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
History
EC 3.4.21.97 created 2000
Orthology
K21078  Betaherpesvirinae capsid scaffolding protein
Reference
1  [PMID:8797829]
  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
Cell 86:835-43 (1996)
DOI:10.1016/S0092-8674(00)80157-9
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
ExplorEnz - The Enzyme Database: 3.4.21.97
IUBMB Enzyme Nomenclature: 3.4.21.97
ExPASy - ENZYME nomenclature database: 3.4.21.97
BRENDA, the Enzyme Database: 3.4.21.97
CAS: 139691-88-6

  All links  
Gene (14)   
   KEGG ORTHOLOGY (1)   
   KEGG GENES (13)   
Protein sequence (1226)   
   UniProt (1122)   
   SWISS-PROT (24)   
   RefSeq(pep) (32)   
   PDBSTR (46)   
   PMD (2)   
DNA sequence (1726)   
   RefSeq(nuc) (32)   
   GenBank (847)   
   EMBL (847)   
3D Structure (17)   
   PDB (17)   
Protein domain (2)   
   InterPro (2)   
All databases (2985)   

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