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Literature summary for 3.4.23.16 extracted from

  • Vance, J.E.; LeBlanc, D.A.; Wingfield, P.; London, R.E.
    Conformational selectivity of HIV-1 protease cleavage of X-Pro peptide bonds and its implications (1997), J. Biol. Chem., 272, 15603-15606.
    View publication on PubMed
Search for more literature for 3.4.23.16

Activating Compound

Activating Compound Comment Organism Structure
cyclophilin human cyclophilin enhances activity, it is proposed that cyclophilin functions as an auxiliary enzyme for the protease during cleavage in the virion Human immunodeficiency virus 1

Protein Variants

Protein Variants Comment Organism
C67A kcat/Km ratio for KARV-Nle-Phe(NO2)-EA-Nle-NH2 as substrate is similar to that of the wild-type enzyme Human immunodeficiency virus 1
C67A/C95A urea denaturation is unchanged from that of the wild-type enzyme. Kcat/Km ratio for KARV-Nle-Phe(NO2)-EA-Nle-NH2 as substrate is similar to that of the wild-type enzyme Human immunodeficiency virus 1

General Stability

General Stability Organism
1.8 M urea, 50% loss of activity of wild-type enzyme and mutant enzyme C67A/C95A Human immunodeficiency virus 1

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.133
-
 KARV-Nle-Phe(NO2)-EA-Nle-NH2 pH 5.0, 25°C, wild-type enzyme Human immunodeficiency virus 1
0.231
-
 KARV-Nle-Phe(NO2)-EA-Nle-NH2 pH 5.0, 25°C, mutant enzyme C95A Human immunodeficiency virus 1
0.244
-
 KARV-Nle-Phe(NO2)-EA-Nle-NH2 pH 5.0, 25°C, mutant enzyme C67A/C95A Human immunodeficiency virus 1
0.263
-
 KARV-Nle-Phe(NO2)-EA-Nle-NH2 pH 5.0, 25°C, mutant enzyme C67A Human immunodeficiency virus 1

Organism

Organism UniProt Comment Textmining
Human immunodeficiency virus 1
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Human immunodeficiency virus 1

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Arg-Glu-[5-[(2'-aminoethyl)-amino]naphthalenesulfonyl]-Ser-Gln-Asn-Tyr-Pro-Ile-Val-Gln-Lys-[4-[[4'-(dimethylamino)phenyl]azo]-benzoyl]-Arg + H2O
-
 Human immunodeficiency virus 1 ?
-
 ?
KARV-Nle-Phe(NO2)-EA-Nle-NH2 + H2O
-
 Human immunodeficiency virus 1 KARV-Nle + Phe(NO2)-EA-Nle-NH2
-
 ?
additional information autocatalytic maturation, two temporally regulated N-terminal cleavages, first at the native TFP/p6pol followed by cleavage at the p6pol/PR, are crucial for protease maturation and enzymatic activity Human immunodeficiency virus 1 ?
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.9
-
 KARV-Nle-Phe(NO2)-EA-Nle-NH2 pH 5.0, 25°C, wild-type enzyme Human immunodeficiency virus 1
3.5
-
 KARV-Nle-Phe(NO2)-EA-Nle-NH2 pH 5.0, 25°C, mutant enzyme C67A/C95A and mutant enzyme C95A Human immunodeficiency virus 1
3.7
-
 KARV-Nle-Phe(NO2)-EA-Nle-NH2 pH 5.0, 25°C, mutant enzyme C67A Human immunodeficiency virus 1