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Literature summary for 3.4.22.62 extracted from

  • Rodriguez, J.; Lazebnik, Y.
    Caspase-9 and APAF-1 form an active holoenzyme (1999), Genes Dev., 13, 3179-3184.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
APAF-1 proteolytic activity of caspase-9 in a complex with APAF-1 is several orders of magnitude higher than that of the free enzyme. Thus, this complex functions as a holoenzyme in which caspase-9 is the catalytic subunit and APAF-1 its allosteric regulator Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
fibroblast
-
Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
IETD-7-amido-4-trifluoromethylcoumarin + H2O
-
Homo sapiens IETD + 7-amino-4-trifluoromethylcoumarin
-
?
pro-caspase-3 + H2O
-
Homo sapiens caspase-3 + ?
-
?
pro-caspase-7 + H2O
-
Homo sapiens caspase-7 + ?
-
?

Subunits

Subunits Comment Organism
More proteolytic activity of caspase-9 in a complex with APAF-1 is several orders of magnitude higher than that of the free enzyme. Thus, this complex functions as a holoenzyme in which caspase-9 is the catalytic subunit and APAF-1 its allosteric regulator Homo sapiens