CATH Classification

Domain Context

CATH Clusters

Superfamily 3.40.50.1460
Functional Family Caspase 9

Enzyme Information

3.4.22.62
Caspase-9.
based on mapping to UniProt P55211
Strict requirement for an Asp residue at position P1 and with a marked preference for His at position P2. It has a preferred cleavage sequence of Leu-Gly-His-Asp-|-Xaa.
-!- Caspase-9 is an initiator caspase, as are caspase-2 (EC 3.4.22.55), caspase-8 (EC 3.4.22.61) 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. -!- An alternatively spliced version of caspase-9 also exists, caspase- 9S, that inhibits apoptosis, similar to the situation found with caspase-2. -!- Phosphorylation of caspase-9 from some species by Akt, a serine- threonine protein kinase, inhibits caspase activity in vitro and caspase activation in vivo. -!- The activity of caspase-9 is increased dramatically upon association with the apoptosome but the enzyme can be activated without proteolytic cleavage. -!- Procaspase-3 is the enzyme's physiological substrate. -!- Belongs to peptidase family C14.

UniProtKB Entries (1)

P55211
CASP9_HUMAN
Homo sapiens
Caspase-9

PDB Structure

PDB 2AR9
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Engineering a Dimeric Caspase-9: A Re-Evaluation of the Induced Proximity Model for Caspase Activation
Chao, Y., Shiozaki, E.N., Srinivassula, S.M., Rigotti, D.J., Fairman, R., Shi, Y.
PLOS BIOL.