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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 ...
Some cells synthesize argininosuccinic acid from citrulline and aspartic acid and use it as a precursor for arginine in the urea cycle (or citrulline-NO cycle), releasing fumarate as a by-product to enter the TCA cycle. The enzyme that catalyzes the reaction is argininosuccinate synthetase. [3] [4]
Citrulline is not one of the 20 standard amino acids encoded by DNA in the genetic code. Instead, it is the result of a post-translational modification . 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.
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Homocitrulline has been suggested as a confounding antigen for rheumatoid arthritis antibodies targeting citrullinated proteins/peptides. [1] Antibodies binding to homocitrulline-containing sequences have been found in rheumatoid arthritis patients' sera [2] [3] More recently, it has been shown that homocitrulline-containing proteins are present in rheumatoid arthritis (RA) joints. [4]
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Ornithine transcarbamylase deficiency also known as OTC deficiency is the most common urea cycle disorder in humans. Ornithine transcarbamylase, the defective enzyme in this disorder, is the final enzyme in the proximal portion of the urea cycle, responsible for converting carbamoyl phosphate and ornithine into citrulline.
L-Ornithine is one of the products of the action of the enzyme arginase on L-arginine, creating urea. Therefore, ornithine is a central part of the urea cycle, which allows for the disposal of excess nitrogen. Ornithine is recycled and, in a manner, is a catalyst. First, ammonia is converted into carbamoyl phosphate (H 2 NC(O)OPO 2−
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