Uricoteley:its nature and origin during the evolution of tetrapod vertebrates.
The hepatic mechanism for detoxication of ammonia formed during amino acid gluconeogenesis in uricotelic vertebrates requires the intramitochondrial synthesis of glutamine by glutamine synthetase. This glutamine then serves as a precursor of uric acid in the cytosol. The evolutionary development of uricoteley thus required the localization of glutamine synthetase in liver mitochondria. The mechanism for the mitochondrial import of glutamine synthetase in uricotelic vertebrate liver is not yet known. Tortoises, extant relatives of the stem reptiles, possess both the ureotelic and uricotelic hepatic systems. It therefore seems likely that the genetic events allowing the mitochondrial localization of glutamine synthetase in liver occurred in the amniote amphibian ancestors of the stem reptiles. The selection of ureoteley by the theropsids and of uricoteley by the sauropsids were major events in the divergence and subsequent evolution of these two lines. Once established in the sauropsid line, uricoteley has persisted through to the higher reptiles, crocodilians, and birds. Uricoteley was in part responsible for the radiation of the archosaurs during the Triassic as a water-conserving mechanism in the adult, thereby allowing them to invade the arid environments of that period. Contrary to dogma, uricoteley was probably of minor significance in the development of the cleidoic egg. Neither mammalian nor avian embryonic liver tissues catabolize amino acids to any great extent, so it is inappropriate to attribute to them a kind of "waste" nitrogen metabolism.
D000641:Ammonia / Q000378:metabolism*; D000818:Animals; D005075:Biological Evolution; D005943:Gluconeogenesis; D005974:Glutamate-Ammonia Ligase / Q000378:metabolism; D008099:Liver / Q000378:metabolism*; D014508:Urea / Q000378:metabolism; D014527:Uric Acid / Q000378:metabolism; D014714:Vertebrates / Q000378:metabolism*
D014527:Uric Acid; D000641:Ammonia; D014508:Urea; D005974:Glutamate-Ammonia Ligase