The enzyme is only active as a homodimer, as each one corresponds to half of the eukaryotic two-lobe enzyme. The two parts each contribute one catalytic aspartyl residue.[1]
Retroviral aspartyl protease is synthesised as part of the pol polyprotein that contains an aspartyl protease, a reverse transcriptase, RNase H and integrase. pol polyprotein undergoes specific enzymatic cleavage to yield the mature proteins.
Not all retroviral aspartyl proteases generated from pol are retropepsins in the strict sense. Spumapepsin from foamy virus is divergent enough to get its own family, MEROPS A9. Many other examples are found in clan AA.
^Pettit SC, Everitt LE, Choudhury S, Dunn BM, Kaplan AH (August 2004). "Initial cleavage of the human immunodeficiency virus type 1 GagPol precursor by its activated protease occurs by an intramolecular mechanism". Journal of Virology. 78 (16): 8477–85. doi:10.1128/JVI.78.16.8477-8485.2004. PMC479095. PMID 15280456.
This article incorporates text from the public domain Pfam and InterPro: IPR001995
December 15, 2023
retroviral, aspartyl, protease, retropepsins, single, domain, aspartyl, proteases, from, retroviruses, retrotransposons, badnaviruses, plant, dsdna, viruses, these, proteases, generally, part, larger, polyprotein, retroviral, proteases, homologous, single, dom. Retroviral aspartyl proteases or retropepsins are single domain aspartyl proteases from retroviruses retrotransposons and badnaviruses plant dsDNA viruses These proteases are generally part of a larger pol or gag polyprotein Retroviral proteases are homologous to a single domain of the two domain eukaryotic aspartyl proteases such as pepsins cathepsins and renins Pfam PF00026 MEROPS A1 Retropepsins are members of MEROPS A2 clan AA All known members are endopeptidases Retroviral aspartyl proteaseHIV 1 protease dimer in white and grey with peptide substrate in black and active site aspartate side chains in red PDB 1KJF IdentifiersSymbolRVPPfamPF00077InterProIPR001995PROSITEPDOC00128MEROPSA2SCOP21ida SCOPe SUPFAMOPM superfamily100OPM protein2q63Membranome532Available protein structures Pfam structures ECOD PDBRCSB PDB PDBe PDBjPDBsumstructure summaryThe enzyme is only active as a homodimer as each one corresponds to half of the eukaryotic two lobe enzyme The two parts each contribute one catalytic aspartyl residue 1 Retroviral aspartyl protease is synthesised as part of the pol polyprotein that contains an aspartyl protease a reverse transcriptase RNase H and integrase pol polyprotein undergoes specific enzymatic cleavage to yield the mature proteins Not all retroviral aspartyl proteases generated from pol are retropepsins in the strict sense Spumapepsin from foamy virus is divergent enough to get its own family MEROPS A9 Many other examples are found in clan AA Human proteins containing this domain editDDI1 DDI2 ERVK6 References edit Pettit SC Everitt LE Choudhury S Dunn BM Kaplan AH August 2004 Initial cleavage of the human immunodeficiency virus type 1 GagPol precursor by its activated protease occurs by an intramolecular mechanism Journal of Virology 78 16 8477 85 doi 10 1128 JVI 78 16 8477 8485 2004 PMC 479095 PMID 15280456 See also editHIV 1 protease Portal nbsp Biology This article incorporates text from the public domain Pfam and InterPro IPR001995 Retrieved from https en wikipedia org w index php title Retroviral aspartyl protease amp oldid 1028761797, wikipedia, wiki, book, books, library,
