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Literature summary for 3.4.23.16 extracted from

  • Ishima, R.; Torchia, D.A.; Louis, J.M.
    Mutational and structural studies aimed at characterizing the monomer of HIV-1 protease and its precursor (2007), J. Biol. Chem., 282, 17190-17199.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
additional information protease lacking the terminal residues 1-4 and 96-99 exhibits a stable monomer fold Human immunodeficiency virus 1
T26A mutation increases the stability of the monomer fold, mutant still exhibits a high Kd value of more than 0.5 mM Human immunodeficiency virus 1

Organic Solvent Stability

Organic Solvent Comment Organism
urea the urea-induced unfolding transition of the protease monomer even lacking the interfacial terminal 4 residues (PR5-95) is similar to that of the pseudo wild-type active or the inactive (PRD25N) dimers with a transition mid-point of about 1.9 M urea 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.
Lys-Ala-Arg-Val-Nle-(4-nitrophenylalanine)-Glu-Ala-Nle-NH2 + H2O
-
Human immunodeficiency virus 1 Lys-Ala-Arg-Val-Nle + (4-nitrophenylalanine)-Glu-Ala-Nle-NH2
-
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Synonyms

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