Peptidase family C14A, His active site QuickView

Description:: Interleukin-1 beta converting enzyme (ICE) is responsiblefor the cleavage of the IL-1 beta precursor at an Asp-Ala bond to generate themature biologically active cytokine. ICE a thiol protease composed of twosubunits of 10 (p10) and 20 Kd (p20), both derived by the autocleavage of a 45Kd precursor (p45). Two residues are implicated in the catalytic mechanism: acysteine and an histidine. They are located in the P20 subunit after cleavageof the precursor. ICE belongs to a family of peptidases which isimplicated in programmed cell death (apoptosis) and which has been termed'caspase' for cysteine aspase. ICE is known as Caspase-1 and the other membersof this family include: Caspase-2 (ICH-1, NEDD-2). Caspase-3 (also known as apopain, CPP32, Yama), a protease which, at the onset of apoptosis, proteolytically cleaves poly(ADP-ribose) polymerase at an Asp-Gly bond. Caspase-4 (ICH-2, TX, ICErel-II). Caspase-5 (ICH-3, TY, ICErel-III). Caspase-6 (MCH-2). Caspase-7 (MCH-3, ICE-LAP3, CMH-1, SCA-2, LICE2). Caspase-8 (MCH-5, MACH, FLICE). Caspase-9 (MCH-6, ICE-LAP6). Caspase-10 (MCH-4, FLICE2). Caspase-11. Caspase-12. Caspase-13 (ERICE). Caspase-14. Caenorhabditis elegans ced-3 involved in the initiation of apoptosis. Drosophila Ice. This entry represents a conserved region containing the histidine active site.

QuickView for Peptidase family C14A, His active site (biogroup)