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Literature summary for 3.4.23.16 extracted from

  • Deshmukh, L.; Tugarinov, V.; Louis, J.M.; Clore, G.M.
    Binding kinetics and substrate selectivity in HIV-1 protease-Gag interactions probed at atomic resolution by chemical exchange NMR (2017), Proc. Natl. Acad. Sci. USA, 114, E9855-E9862 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21-CodonPlus (DE3) RIPL cells Human immunodeficiency virus 1

Protein Variants

Protein Variants Comment Organism
D25N inactive Human immunodeficiency virus 1

Inhibitors

Inhibitors Comment Organism Structure
darunavir
-
Human immunodeficiency virus 1

Localization

Localization Comment Organism GeneOntology No. Textmining

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Human immunodeficiency virus 1
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Gag polyprotein + H2O
-
Human immunodeficiency virus 1 ?
-
?

Synonyms

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

General Information

General Information Comment Organism
physiological function the conversion of immature noninfectious HIV-1 particles to infectious virions is dependent upon the sequential cleavage of the precursor group-specific antigen (Gag) polyprotein by the enzyme Human immunodeficiency virus 1