Hydrolases;
Acting on peptide bonds (peptidases);
Cysteine endopeptidases
Reaction(IUBMB)
Strict requirement for an Asp residue at position P1 and has a preferred cleavage sequence of Tyr-Val-Ala-Asp!
Comment
From mammalian monocytes. This enzyme is part of the family of inflammatory caspases, which also includes caspase-4 (EC 3.4.22.57) and caspase-5 (EC 3.4.22.58) in humans and caspase-11 (EC 3.4.22.64), caspase-12, caspase-13 and caspase-14 in mice. Contains a caspase-recruitment domain (CARD) in its N-terminal prodomain, which plays a role in procaspase activation [6,7]. Cleaves pro-interleukin-1beta (pro-IL-1beta) to form mature IL-1beta, a potent mediator of inflammation. Also activates the proinflammatory cytokine, IL-18, which is also known as interferon-gamma-inducing factor [6]. Inhibited by Ac-Tyr-Val-Ala-Asp-CHO. Caspase-11 plays a critical role in the activation of caspase-1 in mice, whereas caspase-4 enhances its activation in humans [7]. Belongs in peptidase family C14.
History
EC 3.4.22.36 created 1993, modified 1997, modified 2007
Howard AD, Kostura MJ, Thornberry N, Ding GJ, Limjuco G, Weidner J, Salley JP, Hogquist KA, Chaplin DD, Mumford RA, et al.
Title
IL-1-converting enzyme requires aspartic acid residues for processing of the IL-1 beta precursor at two distinct sites and does not cleave 31-kDa IL-1 alpha.
