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Literature summary extracted from

  • Davis, D.A.; Newcomb, F.M.; Moskovitz, J.; Wingfield, P.T.; Stahl, S.J.; Kaufman, J.; Fales, H.M.; Levine, R.L.; Yarchoan, R.
    HIV-2 protease is inactivated after oxidation at the dimer interface and activity can be partly restored with methionine sulphoxide reductase (2000), Biochem. J., 346, 305-311.
No PubMed abstract available

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.4.23.47
-
 Human immunodeficiency virus 2

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.23.47 H2O2 inactivated after oxidation at the dimer interface, activity can be partly restored with methionine sulphoxide reductase Human immunodeficiency virus 2

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.4.23.47 GAG precursor protein of HIV-2 + H2O Human immunodeficiency virus 2
-
 ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.4.23.47 Human immunodeficiency virus 2
-
 human immunodeficiency virus type 2
-

Oxidation Stability

EC Number Oxidation Stability Organism
3.4.23.47 inactivated after oxidation at the dimer interface, activity can be partly restored with methionine sulphoxide reductase Human immunodeficiency virus 2

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.23.47 GAG precursor protein of HIV-2 + H2O
-
 Human immunodeficiency virus 2 ?
-
 ?