Adenain
| Adenain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.4.22.39 | ||||||||
| CAS number | 369652-03-9 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| 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 coded by adenoviruses.
References
- ↑ Webster, A.; Hay, R.T.; Kemp, G. (1993). "The adenovirus protease is activated by a virus-coded disulphide-linked peptide". Cell. 72: 97–104. doi:10.1016/0092-8674(93)90053-s. PMID 8422686.
- ↑ Ding, J.Z.; McGrath, W.J.; Sweet, R.M.; Mangel, W.F. (1996). "Crystal structure of the human adenovirus proteinase with its 11 residue cofactor". EMBO J. 15: 1778–1783. PMID 8617222.
- ↑ Weber, J.M.; Rawlings, N.D.; Woessner, J.F. (1998). "Adenovirus protease". In Barrett, A.J. Handbook of Proteolytic Enzymes. London: Academic Press. pp. 741–743.
External links
- Adenain at the US National Library of Medicine Medical Subject Headings (MeSH)
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