Ubiquitin-activating enzyme
Ubiquitin-activating enzyme
Ubiquitin-activating enzyme (pronounced: yoo-bi-kwit-in ak-tuh-vey-ting en-zahym), also known as E1 enzyme, is a key component in the ubiquitin-proteasome system (UPS). The UPS is a crucial biological pathway in cells that controls the degradation of proteins.
Etymology
The term "ubiquitin" comes from the Latin word ubique, which means "everywhere". This is due to the widespread presence of ubiquitin in all eukaryotic cells. The term "activating enzyme" refers to the role of this enzyme in activating ubiquitin for protein degradation.
Function
Ubiquitin-activating enzyme initiates the ubiquitination process by activating ubiquitin in an ATP-dependent manner. This activation forms a high-energy thioester bond between the C-terminal glycine of ubiquitin and a cysteine residue on the E1 enzyme. The activated ubiquitin is then transferred to a ubiquitin-conjugating enzyme (E2), and finally to the protein substrate with the help of a ubiquitin ligase (E3).
Related Terms
- Ubiquitin: A small protein that is found in all eukaryotic cells. It is used to mark proteins for degradation by the proteasome.
- Ubiquitin-proteasome system: A system within cells that degrades and recycles proteins.
- Ubiquitin-conjugating enzyme: Also known as E2 enzyme, it accepts ubiquitin from the E1 enzyme and transfers it to the protein substrate.
- Ubiquitin ligase: Also known as E3 enzyme, it facilitates the transfer of ubiquitin from the E2 enzyme to the protein substrate.
External links
- Medical encyclopedia article on Ubiquitin-activating enzyme
- Wikipedia's article - Ubiquitin-activating enzyme
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