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Literature summary for 3.4.22.60 extracted from

  • Martini, C.; Bedard, M.; Lavigne, P.; Denault, J.B.
    Characterization of Hsp90 co-chaperone p23 cleavage by caspase-7 uncovers a peptidase-substrate interaction involving intrinsically disordered regions (2017), Biochemistry, 56, 5099-5111 .
    View publication on PubMed
Search for more literature for 3.4.22.60

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0309
-
 N-acetyl-DEVD-7-amido-4-trifluoromethylcoumarin pH 7.2, 37°C Homo sapiens
0.209
-
 N-acetyl-PEVD-7-amido-4-trifluoromethylcoumarin pH 7.2, 37°C Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens P55210
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
N-acetyl-DEVD-7-amido-4-trifluoromethylcoumarin + H2O
-
 Homo sapiens acetyl-DEVD + 7-amino-4-trifluoromethylcoumarin
-
 ?
N-acetyl-PEVD-7-amido-4-trifluoromethylcoumarin + H2O
-
 Homo sapiens acetyl-PEVD + 7-amino-4-trifluoromethylcoumarin
-
 ?
p23 + H2O i.e. Hsp90 cochaperone p23. Residues 36-45 of caspase-7 participate in p23 recognition. The caspase-7 N-terminal domain binds close to the cleavage site in the C-terminal tail of p23, and cleavage occurs at residues PEVD142-G bearing a P4 Pro residue Homo sapiens ?
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.9
-
 N-acetyl-PEVD-7-amido-4-trifluoromethylcoumarin pH 7.2, 37°C Homo sapiens
5.6
-
 N-acetyl-DEVD-7-amido-4-trifluoromethylcoumarin pH 7.2, 37°C Homo sapiens

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
4.3
-
 N-acetyl-PEVD-7-amido-4-trifluoromethylcoumarin pH 7.2, 37°C Homo sapiens
185
-
 N-acetyl-DEVD-7-amido-4-trifluoromethylcoumarin pH 7.2, 37°C Homo sapiens