HIV-1 protease
Enzyme involved with peptide bond hydrolysis in retroviruses / From Wikipedia, the free encyclopedia
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HIV-1 protease or PR is a retroviral aspartyl protease (retropepsin), an enzyme involved with peptide bond hydrolysis in retroviruses, that is essential for the life-cycle of HIV, the retrovirus that causes AIDS.[1][2] HIV-1 PR cleaves newly synthesized polyproteins (namely, Gag and Gag-Pol[3]) at nine cleavage sites to create the mature protein components of an HIV virion, the infectious form of a virus outside of the host cell.[4] Without effective HIV-1 PR, HIV virions remain uninfectious.[5][6]
Quick Facts Identifiers, EC no. ...
HIV-1 Protease (Retropepsin) | |||||||||
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Identifiers | |||||||||
EC no. | 3.4.23.16 | ||||||||
CAS no. | 144114-21-6 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / QuickGO | ||||||||
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