Canadian Medical Guide > Chemicals and Drugs > Enzymes and Coenzymes > Enzymes > Ligases > Ubiquitin-Protein Ligase Complexes Terms and Definitions
Ubiquitin-Protein Ligase Complexes
Medical Definition: | Complexes of enzymes that catalyze the covalent attachment of UBIQUITIN to other proteins by forming a peptide bond between the C-terminal GLYCINE of UBIQUITIN and the alpha-amino groups of LYSINE residues in the protein. The complexes play an important role in mediating the selective-degradation of short-lived and abnormal proteins. The complex of enzymes can be broken down into three components that involve activation of ubiquitin (UBIQUITIN-ACTIVATING ENZYMES), conjugation of ubiquitin to the ligase complex (UBIQUITIN-CONJUGATING ENZYMES), and ligation of ubiquitin to the substrate protein (UBIQUITIN-PROTEIN LIGASES). |
Guide Notes: | UBIQUITIN-PROTEIN LIGASES is also available |
CAS Number: | EC 6.3.2.19 |
Previously Indexed: | Ligases (1983-2003) |
Ubiquitin-Activating Enzymes - A class of enzymes that catalyzes the ATP-dependent formation of a thioester bond between itself and UBIQUITIN. It then transfers the activated ubiquitin to one of the UBIQUITIN-PROTEIN LIGASES. | |
Ubiquitin-Conjugating Enzymes - A class of enzymes that form a thioester bond to UBIQUITIN with the assistance of UBIQUITIN-ACTIVATING ENZYMES. They transfer ubiquitin to the LYSINE of a substrate protein with the assistance of UBIQUITIN-PROTEIN LIGASES. | |
Ubiquitin-Protein Ligases - A diverse class of enzymes that interact with UBIQUITIN-CONJUGATING ENZYMES and ubiquitination-specific protein substrates. Each member of this enzyme group has its own distinct specificity for a substrate and ubiquitin-conjugating enzyme. Ubiquitin-protein ligases exist as both monomeric proteins multiprotein complexes. |
Ubiquitin-Protein Ligase Complexes Medical Definitions and Terms
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