Deubiquitinating Enzymes

Deubiquitinating Enzymes
The ubiquitin-proteasome pathway is an important protein degradation regulatory
system in cells. Through the ubiquitination of substrate proteins and proteasomal
degradation, a variety of cellular activities can be affected or regulated, including:
gene transcription, cell cycle regulation, immune response, cell receptor function,
tumor growth, and inflammatory processes. Due to the extensive and reversible
function of this pathway, it is strictly regulated in the body, and the regulation of
deubiquitinating enzyme is an important link. At present, it is confirmed that there
are many deubiquitinating enzymes in the cells, which are mainly divided into five
types, which are mainly ubiquitin carboxy terminal hydrolase family and
ubiquitin-specific processing enzyme family. These different types of deubiquitinating
enzymes are capable of hydrolyzing the linkages between the ubiquitin chains on the
substrate proteins, deubiquitinating, and inversely regulating protein degradation,
thereby affecting protein function.
Classification of deubiquitinating enzymes
Deubiquitinating enzymes are a large family of proteases. It mainly hydrolyzes
ubiquitin molecules from ubiquitin-linked proteins or precursor proteins by
hydrolyzing ester bonds, peptide bonds or isopeptide bonds at the carboxy terminus
of ubiquitin. A variety of deubiquitinating enzymes have been isolated and identified
from yeast and humans. Based on the structural similarity (ie, amino acid sequence
homology) of these deubiquitinating enzymes and possible mechanisms of action,
the current deubiquitinating enzymes can mainly divide into five types, which are
mainly ubiquitin carboxy terminal hydrolase family and ubiquitin-specific processing
enzyme family.