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Literature summary for 3.4.23.16 extracted from

  • Yu, Y.; Wang, J.; Shao, Q.; Shi, J.; Zhu, W.
    Effects of drug-resistant mutations on the dynamic properties of HIV-1 protease and inhibition by amprenavir and darunavir (2015), Sci. Rep., 5, 10517 .
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
L10I/G48V/I54V/V82A multi-drug-resistant variant Human immunodeficiency virus 1
V82T/I84V multi-drug-resistant variant Human immunodeficiency virus 1

Inhibitors

Inhibitors Comment Organism Structure
amprenavir
-
Human immunodeficiency virus 1
darunavir
-
Human immunodeficiency virus 1

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 Q7SSI0
-
-

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
homodimer
-
Human immunodeficiency virus 1

Synonyms

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

General Information

General Information Comment Organism
physiological function the enzyme is essential to the replication and invasion of HIV and is responsible for cleaving large polyprotein precursors Gag and releasing small structural proteins to help the assembly of infectious viral particles Human immunodeficiency virus 1