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Literature summary for 3.4.23.16 extracted from

  • Potempa, M.; Lee, S.K.; Kurt Yilmaz, N.; Nalivaika, E.A.; Rogers, A.; Spielvogel, E.; Carter, C.W.; Schiffer, C.A.; Swanstrom, R.
    HIV-1 protease uses bi-specific S2/S2 subsites to optimize cleavage of two classes of target sites (2018), J. Mol. Biol., 430, 5182-5195 .
    View publication on PubMedView publication on EuropePMC
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
Gag polyprotein + H2O Human immunodeficiency virus 1
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 ?
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Organism

Organism UniProt Comment Textmining
Human immunodeficiency virus 1
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-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Gag polyprotein + H2O
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 Human immunodeficiency virus 1 ?
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 ?
additional information the enzyme prefers to have large hydrophobic amino acids flanking the scissile bond. When P1' is proline, the P2 side chain interacts with a polar region in the S2 subsite of the enzyme, while the P2' amino acid interacts with a hydrophobic region of the S2' subsite. When P1' is not proline, the orientations of the P2 and P2' side chains with respect to the scissile bond are reversed. P2 residues interact with a hydrophobic face of the S2 subsite, while the P2' amino acid usually engages hydrophilic amino acids in the S2' subsite Human immunodeficiency virus 1 ?
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 ?

Synonyms

Synonyms Comment Organism
HIV-1 PR
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 Human immunodeficiency virus 1
HIV-1 protease
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 Human immunodeficiency virus 1