Literature summary for 3.4.22.64 extracted from

Lee, B.L.; Stowe, I.B.; Gupta, A.; Kornfeld, O.S.; Roose-Girma, M.; Anderson, K.; Warming, S.; Zhang, J.; Lee, W.P.; Kayagaki, N.
Caspase-11 auto-proteolysis is crucial for noncanonical inflammasome activation (2018), J. Exp. Med., 215, 2279-2288 .

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Protein Variants

Protein Variants	Comment	Organism
C254A	enzymatically inactive	Mus musculus
D285A	mutation disrupts the processing site in the linker region between the large and small subunits of caspase-11	Mus musculus

Organism

Organism	UniProt	Comment	Textmining
Mus musculus	P70343	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
gasdermin D + H2O	-	Mus musculus	?	-	?

General Information

General Information	Comment	Organism
metabolism	caspase-11 auto-cleavage at the intersubunit linker is essential for optimal catalytic activity and subsequent proteolytic cleavage of gasdermin D. Macrophages from caspase-11-processing dead KI mice (Casp11Prc D285A/D285A) exhibit defective caspase-11 auto-processing and phenocopy Casp11-/- and caspase-11 enzymatically dead KI (Casp11Enz C254A/C254A) macrophages in attenuating responses to cytoplasmic lipopolysaccharide or Gram-negative bacteria infection. Gasdermin D D276A/D276A KI macrophages also fail to cleave gasdermin D and are hyporesponsive to inflammasome stimuli	Mus musculus

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Release 2023.1 (January 2023)