Adenain
| Adenain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.4.22.39 | ||||||||
| CAS no. | 369652-03-9 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Adenain (EC 3.4.22.39) is an enzyme.[1][2][3] This enzyme catalyses the following chemical reaction
- Cleaves proteins of the adenovirus and its host cell at two consensus sites: -Yaa-Xaa-Gly-Gly-Xaa- and -Yaa-Xaa-Gly-Xaa-Gly- (in which Yaa is Met, Ile or Leu, and Xaa is any amino acid)
This cysteine endopeptidase is encoded by adenoviruses.
References
[edit]- ↑ Webster A, Hay RT, Kemp G (January 1993). "The adenovirus protease is activated by a virus-coded disulphide-linked peptide". Cell. 72 (1): 97–104. doi:10.1016/0092-8674(93)90053-s. PMID 8422686.
- ↑ Ding J, McGrath WJ, Sweet RM, Mangel WF (April 1996). "Crystal structure of the human adenovirus proteinase with its 11 amino acid cofactor". The EMBO Journal. 15 (8): 1778–83. doi:10.1002/j.1460-2075.1996.tb00526.x. PMC 450093. PMID 8617222.
- ↑ Weber, J.M.; Rawlings, N.D.; Woessner, J.F. (1998). "Adenovirus protease". In Barrett, A.J. (ed.). Handbook of Proteolytic Enzymes. London: Academic Press. pp. 741–743.
External links
[edit]- Adenain at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
