Ornithine is an amino acid that plays a role in the urea cycle.
Role in urea cycle
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 (phosphate-CONH2), which creates one half of urea. Ornithine is converted into a urea derivative at the δ (terminal) nitrogen by carbamoyl phosphate. Another nitrogen is added from aspartate, producing the denitrogenated fumarate, and the resulting arginine (a guanidinium compound) is hydrolysed back to ornithine, producing urea. The nitrogens of urea come from the ammonia and aspartate, and the nitrogen in ornithine remains intact.
Ornithine is not an amino acid coded for by DNA, and, in that sense, is not involved in protein synthesis. However, in mammalian non-hepatic tissues, the main use of the urea cycle is in arginine biosynthesis, so, as an intermediate in metabolic processes, ornithine is quite important. It is believed not to be a part of genetic code because polypeptides containing unprotected ornithines undergo spontaneous lactamization.
Ornithine, via the action of ornithine decarboxylase (E.C. 22.214.171.124), is the starting point for the synthesis of polyamines such as putrescine.
In bacteria, such as E. coli, ornithine can be synthesized from L-glutamate.
Ornithine is also the starting point for cocaine biosynthesis, when decarboxylased, then modified greatly by Cytochrome P450.
generation of homocysteine: S-Adenosyl methionine · S-Adenosyl-L-homocysteine · Homocysteine
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