Enzymer som katalyserar förening av glutaminhärledd ammoniak med annan molekyl. Sammankopplingen sker genom en kol-kvävebindning. EC 6.3.5.

Enzymer som katalyserar förening av två molekyler genom bildande av en kol-kvävebindning. EC 6.3.

Ett icke-metalliskt grundämne med kemiskt tecken C, atomnummer 6 och atomvikt 12,011. Kol kan förekomma i olika allotropa former, som t ex diamant, kol och grafit.

Ett gasformigt grundämne med kemiskt tecken N, atomnummer 7 och atomvikt 14. Kvävemolekylen består av en dubbelatom, och gasen utgör ca 78 volymprocent av jordens atmosfär. Kväve är en beståndsdel av proteiner och nukleinsyror, och ingår i alla levande celler.

Enzymer som katalyserar klyvning av kol-kvävebindningar på annat sätt än genom hydrolys eller oxidation. Undergrupper är ammoniaklyaser, amidinlyaser, aminlyaser och andra kol-kvävelyaser. EC 4.3.

Enzymer som katalyserar brott på kol-syrebindningen, vilket leder till uppkomst av omättade ämnen genom förlust av vatten. EC 4.2.1.

Ubiquitin-protein ligases are enzymes that play a crucial role in the ubiquitination process, which is a post-translational modification of proteins. This process involves the covalent attachment of the protein ubiquitin to specific lysine residues on target proteins, thereby marking them for degradation or altering their function, localization, or interaction with other proteins. Ubiquitin-protein ligases catalyze the transfer of ubiquitin from an E2 ubiquitin-conjugating enzyme to the target protein, forming an isopeptide bond between ubiquitin and the target protein. There are several classes of ubiquitin-protein ligases, including HECT (Homologous to the E6-AP Carboxyl Terminus), RING (Really Interesting New Gene), and U-box ligases, which differ in their mechanisms of catalyzing ubiquitination. Dysregulation of ubiquitin-protein ligases has been implicated in various diseases, including cancer, neurodegenerative disorders, and inflammatory conditions.

Poly(deoxiribonukleotid):poly(deoxiribonukleotid)-ligaser. Enzymer som katalyserar hopkopplingen av redan bildade deoxiribonukleotider med fosfodiesterlänkning vid genetiska processer i samband med reparation av enkelsträngsbrott i duplex-DNA. EC 6.5.1.1 (ATP) och EC 6.5.1.2 (NAD).

SCPH (Skp, Cullin, F-box containing) protein ligases are a family of E3 ubiquitin ligase complexes that play a crucial role in the ubiquitination and subsequent degradation of specific cellular proteins. These complexes are composed of three core components: Skp (S-phase kinase associated protein), Cullin, and an F-box protein. The F-box protein serves as a substrate recognition component that binds to the protein to be ubiquitinated, leading to its targeted degradation by the 26S proteasome. SCPH ligases are involved in various cellular processes, including cell cycle regulation, signal transduction, and DNA damage response.

'Cullin proteins' are a family of structual components that play a crucial role in the formation of multi-subunit E3 ubiquitin ligase complexes, which are responsible for targeting specific cellular proteins for degradation via the ubiquitin-proteasome pathway. There are eight known mammalian cullin family members (CUL1, CUL2, CUL3, CUL4A, CUL4B, CUL5, CUL7, and CUL9), each of which associates with distinct sets of proteins to form unique E3 ubiquitin ligase complexes. These complexes regulate various cellular processes, including cell cycle progression, transcriptional regulation, DNA damage response, and signal transduction, by controlling the stability and function of key regulatory proteins through ubiquitination.

Ubiquitination är ett posttranslationellt modifieringssätt som involverar att en ubiquitinprotein kovalent adderas till en targetprotein. Detta process kontrolleras av tre huvudsakliga grupper av enzymkomplex: E1-ubiquitinaktiverande enzymer, E2-ubiquitinkonjugeringsenzymer och E3-ubiquitinligaseringsenzymer. Ubiquitiner kan adderas som en monomer eller i längre kedjor till targetproteinet, vilket kan leda till olika konsekvenser som proteasomdegradering, förändring av subcellulär lokalisation eller förändrad protein-proteininteraktion. Ubiquitination spelar därför en viktig roll i regleringen av cellulära processer såsom signaltransduktion, DNA-reparation och apoptos.

Polynucleotide ligases are enzymes that catalyze the formation of a phosphodiester bond between the 3'-hydroxyl group of one nucleotide and the 5'-phosphate group of another nucleotide, thereby joining two polynucleotide strands together. This process is essential for DNA replication, repair, and recombination.

Ubiquitin är ett litet protein som spelar en viktig roll i cellens proteinska homeostas. Det fungerar som en etikett som kan kopplas till andra proteiner, vilket kan leda till en rad olika konsekvenser, såsom att markera proteinerna för nedbrytning eller att påverka deras funktion och lokalisation inom cellen. Processen att addera ubiquitin kallas ubiquitinering, och den regleras av en komplex maskinapparat bestående av flera olika enzymer. Ubiquitinering är involverad i en rad cellulära processer, såsom proteinsyntes, DNA-reparation, signaltransduktion och celldelning.

'RING finger domains' refer to a type of protein domain characterized by the presence of a zinc-binding motif with the pattern Cys-X-X-Cys-X-X-X-Cys-X-His/Cys, where 'C' represents cysteine, 'H' represents histidine, and 'X' can be any amino acid. These domains are often found in proteins involved in various cellular processes such as ubiquitination, transcription regulation, and DNA repair. They play a crucial role in mediating protein-protein interactions and are named after the finger-like structure they adopt upon binding to zinc ions.

Enzymer som katalyserar bildandet av acyl-CoA-derivat. EC 6.2.1.

Ubiquitin-conjugating enzymes (E2s) are a group of enzymes that play a crucial role in the ubiquitination process, which is a post-translational modification of proteins. This process involves the covalent attachment of the protein ubiquitin to specific lysine residues on target proteins, marking them for degradation by the 26S proteasome. Ubiquitin-conjugating enzymes function as the central components of the ubiquitination machinery, facilitating the transfer of ubiquitin from an E1 ubiquitin-activating enzyme to an E3 ubiquitin ligase, which ultimately leads to the attachment of ubiquitin to the target protein. Dysregulation of the ubiquitination process has been implicated in various diseases, including cancer and neurodegenerative disorders.

F-box proteins are a type of protein that play a crucial role in the ubiquitination and degradation of other cellular proteins. They are characterized by an approximately 40-amino acid motif known as the F-box, which interacts with other components of the Skp1-Cul1-F-box (SCF) complex, a type of E3 ubiquitin ligase. The SCF complex targets specific proteins for degradation by the 26S proteasome, and F-box proteins help to determine which proteins are targeted by recognizing specific motifs or domains within their substrates. There are multiple types of F-box proteins, each with different substrate specificities, allowing for precise control over protein turnover in the cell.