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Literature summary for 3.4.22.60 extracted from

  • Fang, B.; Boross, P.I.; Tozser, J.; Weber, I.T.
    Structural and kinetic analysis of caspase-3 reveals role for S5 binding site in substrate recognition (2006), J. Mol. Biol., 360, 654-666.
    View publication on PubMed
Search for more literature for 3.4.22.60

Application

Application Comment Organism
medicine hydrophobic P5 residue has a favorable contribution to the recognition and hydrolysis of substrates but not by caspase-7, this information helps to design specific inhibitors for each caspase Homo sapiens

Cloned(Commentary)

Cloned (Comment) Organism
-
 Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.2193
-
 Ac-DVAD-p-nitroanilide
-
 Homo sapiens
0.3149
-
 Ac-VDVAD-p-nitroanilide
-
 Homo sapiens
0.3239
-
 Ac-LDVAD-p-nitroanilide
-
 Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Purification (Commentary)

Purification (Comment) Organism
by nickel affinity chromatography, anion exchange chromatography and gel filtration Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Ac-DVAD-p-nitroanilide + H2O
-
 Homo sapiens p-nitroaniline + Ac-DVAD
-
 ?
Ac-LDVAD-p-nitroanilide + H2O
-
 Homo sapiens p-nitroaniline + Ac-LDVAD
-
 ?
Ac-VDVAD-p-nitroanilide + H2O
-
 Homo sapiens p-nitroaniline + Ac-VDVAD
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.9467
-
 Ac-DVAD-p-nitroanilide
-
 Homo sapiens
1.102
-
 Ac-LDVAD-p-nitroanilide
-
 Homo sapiens
1.26
-
 Ac-VDVAD-p-nitroanilide
-
 Homo sapiens
6.08
-
 Ac-DVAD-p-nitroanilide
-
 Homo sapiens
6.08
-
 Ac-LDVAD-p-nitroanilide
-
 Homo sapiens