Ubiquitin Conjugating Enzyme E2E1, also known as UBE2E1, is a member of the E2 ubiquitin-conjugating enzyme family. This enzyme plays a crucial role in the ubiquitination process, which is a fundamental cellular mechanism for targeting abnormal or short-lived proteins for degradation. The human recombinant form of UBE2E1 is produced using recombinant DNA technology, allowing for its use in various research and experimental applications.
UBE2E1 is responsible for accepting ubiquitin from the E1 complex and catalyzing its covalent attachment to other proteins. This process involves the formation of a thioester bond between the ubiquitin molecule and the active site cysteine residue of UBE2E1. The enzyme then transfers the ubiquitin to the target protein, facilitating its degradation via the proteasome pathway .
In addition to its role in protein degradation, UBE2E1 also catalyzes the covalent attachment of ISG15, a ubiquitin-like modifier, to target proteins. This modification is involved in various cellular processes, including antiviral responses and immune regulation .
The ubiquitination process involves three main classes of enzymes:
The human recombinant form of UBE2E1 is widely used in research to study the ubiquitination process and its implications in various diseases. It serves as a valuable tool for investigating the molecular mechanisms underlying protein degradation and the role of ubiquitination in cellular regulation .