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Literature summary extracted from

  • da Cunha, J.P.; Galante, P.A.; de Souza, S.J.
    Different evolutionary strategies for the origin of caspase-1 inhibitors (2008), J. Mol. Evol., 66, 591-597.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.4.22.36 additional information association of RIP2 with CASP-1 via their homologous CARD domain accelerates the processing of CASP-1 into an active enzyme Homo sapiens
3.4.22.36 additional information association of RIP2 with CASP-1 via their homologous CARD domain accelerates the processing of CASP-1 into an active enzyme Macaca mulatta
3.4.22.36 additional information association of RIP2 with CASP-1 via their homologous CARD domain accelerates the processing of CASP-1 into an active enzyme Pan troglodytes

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.4.22.36 DNA sequence analysis Homo sapiens
3.4.22.36 DNA sequence analysis Macaca mulatta
3.4.22.36 DNA sequence analysis Pan troglodytes

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.22.36 additional information caspase 1 inhibitors share sequence similarity to CASP-1 itself and are all mapped to chr11q22.3, overview Homo sapiens
3.4.22.36 additional information caspase 1 inhibitors share sequence similarity to CASP-1 itself and are all mapped to chr11q22.3, overview Macaca mulatta
3.4.22.36 additional information caspase 1 inhibitors share sequence similarity to CASP-1 itself and are all mapped to chr11q22.3, overview Pan troglodytes

Organism

EC Number Organism UniProt Comment Textmining
3.4.22.36 Homo sapiens
-
-
-
3.4.22.36 Macaca mulatta
-
-
-
3.4.22.36 Pan troglodytes
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.4.22.36 proteolytic modification CASP-1 is synthesized as an inactive zymogen and active caspase-1 is produced by proteolytic cleavage of its pro domain, which contains the CAspase Recruitment Domain, i.e. CARD, the CARD domain is localized at the amino end of CASP-1 and serves as a protein-protein interaction module that is important in protein recruitment and proteolytic activation, association of RIP2 with CASP-1 via their homologous CARD domain accelerates the processing of CASP-1 into an active enzyme Homo sapiens
3.4.22.36 proteolytic modification CASP-1 is synthesized as an inactive zymogen and active caspase-1 is produced by proteolytic cleavage of its pro domain, which contains the CAspase Recruitment Domain, i.e. CARD, the CARD domain is localized at the amino end of CASP-1 and serves as a protein-protein interaction module that is important in protein recruitment and proteolytic activation, association of RIP2 with CASP-1 via their homologous CARD domain accelerates the processing of CASP-1 into an active enzyme Macaca mulatta
3.4.22.36 proteolytic modification CASP-1 is synthesized as an inactive zymogen and active caspase-1 is produced by proteolytic cleavage of its pro domain, which contains the CAspase Recruitment Domain, i.e. CARD, the CARD domain is localized at the amino end of CASP-1 and serves as a protein-protein interaction module that is important in protein recruitment and proteolytic activation, association of RIP2 with CASP-1 via their homologous CARD domain accelerates the processing of CASP-1 into an active enzyme Pan troglodytes

Synonyms

EC Number Synonyms Comment Organism
3.4.22.36 CASP-1
-
 Homo sapiens
3.4.22.36 CASP-1
-
 Macaca mulatta
3.4.22.36 CASP-1
-
 Pan troglodytes
3.4.22.36 IL-1B converting enzyme
-
 Homo sapiens
3.4.22.36 IL-1B converting enzyme
-
 Macaca mulatta
3.4.22.36 IL-1B converting enzyme
-
 Pan troglodytes
3.4.22.36 interleukin-1B converting enzyme
-
 Homo sapiens
3.4.22.36 interleukin-1B converting enzyme
-
 Macaca mulatta
3.4.22.36 interleukin-1B converting enzyme
-
 Pan troglodytes