Deubiquitinating enzyme

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Deubiquitinating Enzyme

Deubiquitinating enzymes (DUBs; pronounced: /djuːˈbɪkwɪtɪneɪtɪŋ ˈɛnzaɪmz/), also known as deubiquitinases, are a large group of proteases that cleave ubiquitin from proteins and other molecules. Ubiquitin is a small protein that can be attached to proteins to modify their function.

Etymology

The term "deubiquitinating enzyme" is derived from the action of these enzymes. "De-" is a prefix indicating removal or reversal, "ubiquitin" refers to the small protein that is removed, and "-ating enzyme" indicates that this is an enzyme that performs this action.

Function

DUBs are involved in several cellular processes, including protein degradation, cell cycle control, DNA repair, and signal transduction. They are crucial for maintaining protein homeostasis by removing ubiquitin from proteins, thereby preventing their degradation by the proteasome. This process is also important for regulating the activity of many proteins.

Classification

DUBs are classified into five families based on their sequence and structural similarities: the ubiquitin-specific proteases (USPs), the ubiquitin C-terminal hydrolases (UCHs), the ovarian tumor proteases (OTUs), the Machado-Joseph disease protein domain proteases (MJDs), and the JAB1/MPN/Mov34 metalloenzymes (JAMMs).

Related Terms

  • Ubiquitin: A small protein that can be attached to proteins to modify their function.
  • Protease: An enzyme that performs proteolysis, protein catabolism by hydrolysis of peptide bonds.
  • Proteasome: A protein complex inside all eukaryotes and archaea, and in some bacteria.
  • Cell cycle: The series of events that take place in a cell leading to its division and duplication.
  • DNA repair: A collection of processes by which a cell identifies and corrects damage to the DNA molecules that encode its genome.
  • Signal transduction: The process by which a chemical or physical signal is transmitted through a cell as a series of molecular events.

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