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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−
18416 Ensembl ENSG00000036473 ENSMUSG00000031173 UniProt P00480 P11725 RefSeq (mRNA) NM_000531 NM_008769 RefSeq (protein) NP_000522 NP_032795 Location (UCSC) Chr X: 38.35 – 38.42 Mb Chr X: 10.12 – 10.19 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Ornithine transcarbamylase (OTC) (also called ornithine carbamoyltransferase) is an enzyme (EC 2.1.3.3) that catalyzes the reaction ...
The enzyme ornithine decarboxylase (EC 4.1.1.17, ODC) catalyzes the decarboxylation of ornithine (a product of the urea cycle) to form putrescine. This reaction is the committed step in polyamine synthesis. [1] In humans, this protein has 461 amino acids and forms a homodimer. [2] In humans, ornithine decarboxylase (ODC) is expressed by the ...
The urea cycle (also known as the ornithine cycle) is a cycle of biochemical reactions that produces urea (NH 2) 2 CO from ammonia (NH 3). Animals that use this cycle, mainly amphibians and mammals, are called ureotelic .
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 .
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 ...
Ornithine aminotransferase (OAT) is an enzyme which is encoded in human by the OAT gene located on chromosome 10. The OAT involved in the ultimate formation of the non-essential amino acid proline from the amino acid ornithine. Ornithine aminotransferase forms the initial intermediate in this process. It catalyzes the reverse reaction as well ...
From a kinetic standpoint, cis–trans proline isomerization is a very slow process that can impede the progress of protein folding by trapping one or more proline residues crucial for folding in the non-native isomer, especially when the native protein requires the cis isomer.