Assemblin (EC 3.4.21.97) is an enzyme with systematic name.[1][2] This enzyme catalyses the following chemical reaction
| Assemblin | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.4.21.97 | ||||||||
| CAS no. | 139691-88-6 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
- Cleaves -Ala-Ser- and -Ala-Ala- bonds in the scaffold protein
This enzyme is coded by the herpes-virus virion.
References
edit- ^ Chen P, Tsuge H, Almassy RJ, Gribskov CL, Katoh S, Vanderpool DL, Margosiak SA, Pinko C, Matthews DA, Kan CC (September 1996). "Structure of the human cytomegalovirus protease catalytic domain reveals a novel serine protease fold and catalytic triad". Cell. 86 (5): 835–43. doi:10.1016/s0092-8674(00)80157-9. PMID 8797829.
- ^ Darke PL, Rawlings ND, Woessner JF (1998). "Herpesvirus assemblin". In Barrett AJ (ed.). Handbook of Proteolytic Enzymes. London: Academic Press. pp. 470–472.
External links
edit- Assemblin at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
