ENZYME

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ENZYME entry: EC 3.4.22.55

Accepted Name

Caspase-2.

Alternative Name(s)

CASP-2.

ICH-1.

NEDD-2.

NEDD2 protein.

Neural precursor cell expressed developmentally down-regulated protein 2.

Reaction catalysed

Strict requirement for an Asp residue at P1, with 316-asp being essential for proteolytic activity and has a preferred cleavage sequence of Val-Asp-Val-Ala-Asp-|-

Comment(s)

Caspase-2 is an initiator caspase, as are caspases-8 (EC 3.4.22.61), caspase-9 (EC 3.4.22.62) and caspase-10 (EC 3.4.22.63).
Contains a caspase-recruitment domain (CARD) in its N-terminal prodomain, which plays a role in procaspase activation.
Two forms of caspase-2 exist that have antagonistic effects: caspase- 2L induces programd cell death and caspase-2S suppresses cell death.
Caspase-2 is activated by caspase-3 (EC 3.4.22.56), or by a caspase- 3-like protease.
Activation involves cleavage of the N-terminal prodomain, followed by self-proteolysis between the large and small subunits of pro-caspase- 2 and further proteolysis into smaller fragments.
Proteolysis occurs at Asp residues and the preferred substrate for this enzyme is a pentapeptide rather than a tetrapeptide.
Apart from itself, the enzyme can cleave golgin-16, which is present in the Golgi complex and has a cleavage site that is unique for caspase-2.
Alpha-II-spectrin, a component of the membrane cytoskeleton, is a substrate of the large isoform of pro-caspase-2 (caspase-2L) but not of the short isoform (caspase-2S).
Belongs to peptidase family C14.