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Literature summary for 3.4.23.B8 extracted from

  • Davis, D.A.; Brown, C.A.; Newcomb, F.M.; Boja, E.S.; Fales, H.M.; Kaufman, J.; Stahl, S.J.; Wingfield, P.; Yarchoan, R.
    Reversible oxidative modification as a mechanism for regulating retroviral protease dimerization and activation (2003), J. Virol., 77, 3319-3325.
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
L49I autoproteolysis resistant mutant enzyme. KM-values and turnover-numbers are comparable to that of wild-type enzyme Human T-cell leukemia virus type I

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.03
-
KGPPVILPIQAP pH 5.6, 37°C, wild-type enzyme Human T-cell leukemia virus type I
0.032
-
KTKVLVVQPK pH 5.6, 37°C, mutant enzyme L40I Human T-cell leukemia virus type I
0.033
-
KTKVLVVQPK pH 5.6, 37°C, wild-type enzyme Human T-cell leukemia virus type I
0.034
-
KGPPVILPIQAP pH 5.6, 37°C, mutant enzyme L40I Human T-cell leukemia virus type I
0.098
-
APQVLPVMHP pH 5.6, 37°C, mutant enzyme L40I Human T-cell leukemia virus type I
0.115
-
APQVLPVMHP pH 5.6, 37°C, wild-type enzyme Human T-cell leukemia virus type I
0.23
-
DPASILPVIP pH 5.6, 37°C, wild-type enzyme Human T-cell leukemia virus type I
0.244
-
DPASILPVIP pH 5.6, 37°C, mutant enzyme L40I Human T-cell leukemia virus type I

Organism

Organism UniProt Comment Textmining
Human T-cell leukemia virus type I
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
additional information formation of a disulfide bridge, reversible oxidative modification as a mechanism for regulating retroviral protease dimerization and activation, regulation through reversible glutathionylation of its two conserved cysteine residues Human T-cell leukemia virus type I

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
APQVLPVMHP + H2O
-
Human T-cell leukemia virus type I APQVL + PVMHP
-
?
DPASILPVIP + H2O
-
Human T-cell leukemia virus type I DPASIL + PVIP
-
?
KTKVLVVQPK + H2O
-
Human T-cell leukemia virus type I KTKVL + VVQPK
-
?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.62
-
DPASILPVIP pH 5.6, 37°C, mutant enzyme L40I Human T-cell leukemia virus type I
0.7
-
DPASILPVIP pH 5.6, 37°C, wild-type enzyme Human T-cell leukemia virus type I
5.15
-
KTKVLVVQPK pH 5.6, 37°C, wild-type enzyme Human T-cell leukemia virus type I
5.18
-
KTKVLVVQPK pH 5.6, 37°C, mutant enzyme L40I Human T-cell leukemia virus type I
6.26
-
KGPPVILPIQAP pH 5.6, 37°C, mutant enzyme L40I Human T-cell leukemia virus type I
6.78
-
APQVLPVMHP pH 5.6, 37°C, mutant enzyme L40I Human T-cell leukemia virus type I
6.91
-
KGPPVILPIQAP pH 5.6, 37°C, wild-type enzyme Human T-cell leukemia virus type I
8.67
-
APQVLPVMHP pH 5.6, 37°C, wild-type enzyme Human T-cell leukemia virus type I