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Literature summary for 3.4.22.64 extracted from

  • Devant, P.; Dong, Y.; Mintseris, J.; Ma, W.; Gygi, S.P.; Wu, H.; Kagan, J.C.
    Structural insights into cytokine cleavage by inflammatory caspase-4 (2023), Nature, 624, 451-459.
    View publication on PubMed
Search for more literature for 3.4.22.64

Protein Variants

Protein Variants Comment Organism
K286Y/L287K/S288T site-directed mutagenesis Mus musculus
K343T/A344P/S345R/I346A/H347K/S348A site-directed mutagenesis Mus musculus
additional information structure-based engineering of caspase-11 to generate a model of a hypothetical caspase-11-pro-IL-18 complex. this complex, critical exosite residues Trp263 and Arg265 (corresponding to Trp267 and Arg269 in caspase-4) fit into the hydrophobic pocket in pro-IL-18. Introducing caspase-4-specific mutations at His352 and Leu289 in caspase-11 increases its ability to cleave pro-IL-18 in vitro to a level similar to caspase-4 Mus musculus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
mouse interleukin-18 + H2O Mus musculus low activity ?
-
 ?

Organism

Organism UniProt Comment Textmining
Mus musculus P70343 cf. caspase-4, EC 3.4.22.57
-

Source Tissue

Source Tissue Comment Organism Textmining
additional information mouse caspase-11 is not recruited into inflammasomes Mus musculus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
human interleukin-18 + H2O
-
 Mus musculus ?
-
 ?
additional information mouse caspase-11 cannot cleave IL-1beta efficiently Mus musculus ?
-
-
mouse interleukin-18 + H2O low activity Mus musculus ?
-
 ?

General Information

General Information Comment Organism
evolution the regions surrounding Lys356 and Lys293 in caspase-4, EC 3.4.22.57, which interact with Glu28 and Asp30 in pro-IL-18, are not conserved in caspase-11. Instead, caspase-11 displays non-charged residues (His352 and Leu289) at these sites Mus musculus
metabolism mouse caspase-11 is not recruited into inflammasomes and cannot cleave IL-1beta efficiently, in contrast to human caspase-4 and caspase-5. Human caspase-4 and its mouse homologue caspase-11 possess low activity towards mouse pro-IL-18, whereas human and mouse caspase-1 cleave mouse pro-IL-18 efficiently. Analogous enzymes from dog, lemur, rabbit, and sheep cleave species-matched pro-IL-18 homologues with an efficiency comparable to human caspase-4 cleavage of human pro-IL18 Mus musculus
physiological function in contrast to the human enzyme, mouse caspase-11 does not function as a sensor and effector that mediates cleavage and release of IL-18, and is not involved in canonical inflammasomes Mus musculus