Interleukin-1 beta converting enzyme: a novel cysteine protease required for IL-1 beta production and implicated in programmed cell death. 1995

N A Thornberry, and S M Molineaux
Department of Enzymology, Merck Research Laboratories, Rahway, New Jersey 07065, USA.

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.

UI MeSH Term Description Entries
D007375 Interleukin-1 A soluble factor produced by MONOCYTES; MACROPHAGES, and other cells which activates T-lymphocytes and potentiates their response to mitogens or antigens. Interleukin-1 is a general term refers to either of the two distinct proteins, INTERLEUKIN-1ALPHA and INTERLEUKIN-1BETA. The biological effects of IL-1 include the ability to replace macrophage requirements for T-cell activation. IL-1,Lymphocyte-Activating Factor,Epidermal Cell Derived Thymocyte-Activating Factor,Interleukin I,Macrophage Cell Factor,T Helper Factor,Epidermal Cell Derived Thymocyte Activating Factor,Interleukin 1,Lymphocyte Activating Factor
D008958 Models, Molecular Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures. Molecular Models,Model, Molecular,Molecular Model
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D011487 Protein Conformation The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain). Conformation, Protein,Conformations, Protein,Protein Conformations
D011499 Protein Processing, Post-Translational Any of various enzymatically catalyzed post-translational modifications of PEPTIDES or PROTEINS in the cell of origin. These modifications include carboxylation; HYDROXYLATION; ACETYLATION; PHOSPHORYLATION; METHYLATION; GLYCOSYLATION; ubiquitination; oxidation; proteolysis; and crosslinking and result in changes in molecular weight and electrophoretic motility. Amino Acid Modification, Post-Translational,Post-Translational Modification,Post-Translational Protein Modification,Posttranslational Modification,Protein Modification, Post-Translational,Amino Acid Modification, Posttranslational,Post-Translational Amino Acid Modification,Post-Translational Modifications,Post-Translational Protein Processing,Posttranslational Amino Acid Modification,Posttranslational Modifications,Posttranslational Protein Processing,Protein Processing, Post Translational,Protein Processing, Posttranslational,Amino Acid Modification, Post Translational,Modification, Post-Translational,Modification, Post-Translational Protein,Modification, Posttranslational,Modifications, Post-Translational,Modifications, Post-Translational Protein,Modifications, Posttranslational,Post Translational Amino Acid Modification,Post Translational Modification,Post Translational Modifications,Post Translational Protein Modification,Post Translational Protein Processing,Post-Translational Protein Modifications,Processing, Post-Translational Protein,Processing, Posttranslational Protein,Protein Modification, Post Translational,Protein Modifications, Post-Translational
D003546 Cysteine Endopeptidases ENDOPEPTIDASES which have a cysteine involved in the catalytic process. This group of enzymes is inactivated by CYSTEINE PROTEINASE INHIBITORS such as CYSTATINS and SULFHYDRYL REAGENTS.
D004789 Enzyme Activation Conversion of an inactive form of an enzyme to one possessing metabolic activity. It includes 1, activation by ions (activators); 2, activation by cofactors (coenzymes); and 3, conversion of an enzyme precursor (proenzyme or zymogen) to an active enzyme. Activation, Enzyme,Activations, Enzyme,Enzyme Activations
D000595 Amino Acid Sequence The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D013379 Substrate Specificity A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts. Specificities, Substrate,Specificity, Substrate,Substrate Specificities
D015853 Cysteine Proteinase Inhibitors Exogenous and endogenous compounds which inhibit CYSTEINE ENDOPEPTIDASES. Acid Cysteine Proteinase Inhibitor,Cysteine Protease Inhibitor,Cysteine Protease Inhibitors,Cysteine Proteinase Antagonist,Cysteine Proteinase Antagonists,Cysteine Proteinase Inhibitor,Cysteine Proteinase Inhibitors, Endogenous,Cysteine Proteinase Inhibitors, Exogenous,alpha-Cysteine Protease Inhibitor,Acid Cysteine Proteinase Inhibitors,alpha-Cysteine Protease Inhibitors,Antagonist, Cysteine Proteinase,Antagonists, Cysteine Proteinase,Inhibitor, Cysteine Protease,Inhibitor, Cysteine Proteinase,Inhibitor, alpha-Cysteine Protease,Inhibitors, Cysteine Protease,Inhibitors, Cysteine Proteinase,Inhibitors, alpha-Cysteine Protease,Protease Inhibitor, Cysteine,Protease Inhibitor, alpha-Cysteine,Protease Inhibitors, Cysteine,Protease Inhibitors, alpha-Cysteine,Proteinase Antagonist, Cysteine,Proteinase Antagonists, Cysteine,Proteinase Inhibitor, Cysteine,Proteinase Inhibitors, Cysteine,alpha Cysteine Protease Inhibitor,alpha Cysteine Protease Inhibitors

Related Publications

N A Thornberry, and S M Molineaux
February 1996, European journal of biochemistry,
N A Thornberry, and S M Molineaux
January 1996, Advances in experimental medicine and biology,
N A Thornberry, and S M Molineaux
January 1997, Journal of cellular biochemistry,
N A Thornberry, and S M Molineaux
August 1996, The Journal of experimental medicine,
N A Thornberry, and S M Molineaux
January 1994, Methods in enzymology,
N A Thornberry, and S M Molineaux
August 1992, Archives of biochemistry and biophysics,
Copied contents to your clipboard!