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Literature summary for 3.4.23.47 extracted from

  • Louis, J.M.; Ishima, R.; Aniana, A.; Sayer, J.M.
    Revealing the dimer dissociation and existence of a folded monomer of the mature HIV-2 protease (2009), Protein Sci., 18, 2442-2453.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.23.47

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli Human immunodeficiency virus 2

Protein Variants

Protein Variants Comment Organism
D25N inactive mutant forms a dimer Human immunodeficiency virus 2
DELTA96-99 dimer interface mutations such as a deletion of the C-terminal residues 96-99 (PR21-95), drastically increase the Kd. Deletion mutant consists predominantly of folded monomers. Addition of 2fold excess active-site inhibitor does not promote dimerization Human immunodeficiency virus 2
E37K mutation significantly retards autoproteolytic cleavage during expression. Mutant shows a higher dimer dissociation constant, Kd, compared to wild-type. Km and kcat values for substrate Lys-Ala-Arg-Val-Nle-(4-nitrophenylalanine)-Glu-Ala-Nle comparable to wild-type Human immunodeficiency virus 2
T26A dimer interface mutations in the active site of PR2 drastically increase the Kd. T26A consists predominantly of folded monomers. Addition of 2fold excess active-site inhibitor promotes dimerization of mutant PR2T26A Human immunodeficiency virus 2

Inhibitors

Inhibitors Comment Organism Structure
darunavir
-
 Human immunodeficiency virus 2

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.071
-
 Lys-Ala-Arg-Val-Nle-(4-nitrophenylalanine)-Glu-Ala-Nle mutant E37K2, pH 5.0, 28°C Human immunodeficiency virus 2
0.072
-
 Lys-Ala-Arg-Val-Nle-(4-nitrophenylalanine)-Glu-Ala-Nle wild-type PR2, pH 5.0, 28°C Human immunodeficiency virus 2

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Human immunodeficiency virus 2 enzyme undergoes autoproteolysis at pH 3 at the G35/I36 site ?
-
 ?

Organism

Organism UniProt Comment Textmining
Human immunodeficiency virus 2
-
-
-

Storage Stability

Storage Stability Organism
4°C, phosphate buffer pH 6 and 50 mM NaCl, 72 h, no loss of activity Human immunodeficiency virus 2

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Lys-Ala-Arg-Val-Nle-(4-nitrophenylalanine)-Glu-Ala-Nle + H2O
-
 Human immunodeficiency virus 2 ?
-
 ?
additional information enzyme undergoes autoproteolysis at pH 3 at the G35/I36 site Human immunodeficiency virus 2 ?
-
 ?

Synonyms

Synonyms Comment Organism
HIV-2 protease
-
 Human immunodeficiency virus 2
PR2
-
 Human immunodeficiency virus 2

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
28
-
 assay at Human immunodeficiency virus 2

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
-
 Tm: 60.5°C, binding of darunavir increases Tm by 14.8°C Human immunodeficiency virus 2

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
5.6
-
 Lys-Ala-Arg-Val-Nle-(4-nitrophenylalanine)-Glu-Ala-Nle mutant E37K2, pH 5.0, 28°C Human immunodeficiency virus 2
6.4
-
 Lys-Ala-Arg-Val-Nle-(4-nitrophenylalanine)-Glu-Ala-Nle wild-type PR2, pH 5.0, 28°C Human immunodeficiency virus 2

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
3
-
 enzyme undergoes autoproteolysis at pH 3 at the G35/I36 site Human immunodeficiency virus 2
5
-
 assay at Human immunodeficiency virus 2