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Citrullination is distinct from the formation of the free amino acid citrulline as part of the urea cycle or as a byproduct of enzymes of the nitric oxide synthase family. Enzymes called arginine deiminases (ADIs) catalyze the deimination of free arginine, while protein arginine deiminases or peptidylarginine deiminases (PADs) replace the ...
The organic compound citrulline is an α-amino acid. [2] Its name is derived from citrullus, the Latin word for watermelon.Although named and described by gastroenterologists since the late 19th century, it was first isolated from watermelon in 1914 by Japanese researchers Yatarō Koga (古賀彌太郎) and Ryō Ōtake (大嶽了) [3] [4] and further codified by Mitsunori Wada of Tokyo ...
Histone-modifying enzymes that induce a modification (e.g., add a functional group) are dubbed writers, while enzymes that revert modifications are dubbed erasers. Furthermore, there are many uncommon histone modifications including O-GlcNAcylation, [9] sumoylation, [10] ADP-ribosylation, [11] citrullination [12] [13] [14] and proline ...
In enzymology, a citrullinase (EC 3.5.1.20) is an enzyme that catalyzes the chemical reaction. L-citrulline + H 2 O L-ornithine + CO 2 + NH 3. Thus, the two substrates of this enzyme are L-citrulline and H 2 O, whereas its 3 products are L-ornithine, CO 2, and NH 3.
This gene is a member of a gene family which encodes enzymes responsible for the conversion of arginine to citrulline residues (citrullination).This gene may play a role in granulocyte and macrophage development leading to inflammation and immune response. [6]
Phosphorylation is highly effective for controlling the enzyme activity and is the most common change after translation. [2] Many eukaryotic and prokaryotic proteins also have carbohydrate molecules attached to them in a process called glycosylation, which can promote protein folding and improve stability as well as serving regulatory functions.
Histones are subject to post translational modification by enzymes primarily on their N-terminal tails, but also in their globular domains. [20] [21] Such modifications include methylation, citrullination, acetylation, phosphorylation, SUMOylation, ubiquitination, and ADP-ribosylation. This affects their function of gene regulation.
Vimentin, fibrin, filaggrin, enolase and keratin are common citrullination targets. The list of proteins that undergo citrullination and make up the citrullinome continues to increase. The RA associated citrullinome has been reported to include targets from synovial fluid and tissue that range from proteases, receptors, and carrier proteins.