Interleukin-1 beta converting enzyme: a novel cysteine protease required for IL-1 beta production and implicated in programmed cell death.
Interleukin-1 beta converting enzyme is the first member of a new class of cysteine proteases. The most distinguishing feature of this family is a nearly absolute specificity for cleavage at aspartic acid. This enzyme has been the subject of intense research because of its role in the production of IL-1 beta, a key mediator of inflammation. These studies have culminated in the design of potent inhibitors and determination of its crystal structure. The structure secures the relationship of the enzyme to CED-3, the product of a gene required for programmed cell death in Caenorhabditis elegans, suggesting that members of this family function in cell death in vertebrates.
Thornberry
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NA
Department of Enzymology, Merck Research Laboratories, Rahway, New Jersey 07065, USA.
Molineaux
S M
SM
D000595:Amino Acid Sequence; D017209:Apoptosis / Q000502:physiology*; D020170:Caspase 1; D003546:Cysteine Endopeptidases / Q000737:chemistry / Q000378:metabolism*; D015853:Cysteine Proteinase Inhibitors / Q000494:pharmacology; D004789:Enzyme Activation; D007375:Interleukin-1 / Q000378:metabolism*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D011499:Protein Processing, Post-Translational; D013379:Substrate Specificity
D015853:Cysteine Proteinase Inhibitors; D007375:Interleukin-1; D003546:Cysteine Endopeptidases; D020170:Caspase 1