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Literature summary extracted from

  • Davis, D.A.; Dorsey, K.; Wingfield, P.T.; Stahl, S.J.; Kaufman, J.; Fales, H.M.; Levine, R.L.
    Regulation of HIV-1 protease activity through cysteine modification (1996), Biochemistry, 35, 2482-2488.
    View publication on PubMed

General Stability

EC Number General Stability Organism
3.4.23.16 glutathiolation at Cys67 markedly stabilizes the enzyme activity presumably by reducing autoproteolysis Human immunodeficiency virus 1

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.23.16 5,5'-dithiobis(2-nitrobenzoic acid) enzyme activity is lost when a mixed disulfide is formed between 5,5'-dithiobis(2-nitrobenzoic acid) and Cys95, the same mixed disulfide at Cys67 reduces activity by 50%. Normal activity can be restored when the enzyme is treated with dithiothreitol Human immunodeficiency virus 1

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.4.23.16 10870
-
electrospray mass spectrometry, unmodified protease Human immunodeficiency virus 1

Organism

EC Number Organism UniProt Comment Textmining
3.4.23.16 Human immunodeficiency virus 1
-
produced in Escherichia coli
-
3.4.23.16 Human immunodeficiency virus 1 HXB2
-
produced in Escherichia coli
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.23.16
-
Human immunodeficiency virus 1