Human endogenous retrovirus K endopeptidase
 | This article may be too technical for most readers to understand. (June 2020) |
| Human endogenous retrovirus K endopeptidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.4.23.50 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Human endogenous retrovirus K endopeptidase (EC 3.4.23.50, human endogenous retrovirus K10 endopeptidase, endogenous retrovirus HERV-K10 putative protease, human endogenous retrovirus K retropepsin, HERV K10 endopeptidase, HERV K10 retropepsin, HERV-K PR, HERV-K protease, HERV-K113 protease, human endogenous retrovirus K113 protease, human retrovirus K10 retropepsin) is an enzyme derived from an endogenous retrovirus.[1] This enzyme catalyses the following chemical reaction:
- Processing at the authentic HIV-1 PR recognition site and release of the mature p17 matrix and the p24 capsid protein, as a result of the cleavage of the -SQNY-PIVQ- cleavage site.
This enzyme belongs to the peptidase family A2 (retropepsins).
References
[edit]- ^ Towler EM, Gulnik SV, Bhat TN, Xie D, Gustschina E, Sumpter TR, Robertson N, Jones C, Sauter M, Mueller-Lantzsch N, Debouck C, Erickson JW (December 1998). "Functional characterization of the protease of human endogenous retrovirus, K10: can it complement HIV-1 protease?". Biochemistry. 37 (49): 17137–44. doi:10.1021/bi9818927. PMID 9860826.
External links
[edit]- Human endogenous retrovirus K endopeptidase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
