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Pathway Description
Ammonia Recycling
Homo sapiens
Metabolic Pathway
Created: 2013-08-01
Last Updated: 2023-10-25
Ammonia can be rerouted from the urine and recycled into the body for use in nitrogen metabolism. Glutamate and glutamine play an important role in this process. There are many other processes that act to recycle ammonia. asparaginase recycles ammonia from asparagine. Glycine cleavage system generates ammonia from glycine. Histidine ammonia lyase forms ammonia from histidine. Serine dehydratase also produces ammonia by cleaving serine.
References
Ammonia Recycling References
Lehninger, A.L. Lehninger principles of biochemistry (4th ed.) (2005). New York: W.H Freeman.
Salway, J.G. Metabolism at a glance (3rd ed.) (2004). Alden, Mass.: Blackwell Pub.
Kikuchi G: The glycine cleavage system: composition, reaction mechanism, and physiological significance. Mol Cell Biochem. 1973 Jun 27;1(2):169-87.
Pubmed: 4585091
Saparov SM, Liu K, Agre P, Pohl P: Fast and selective ammonia transport by aquaporin-8. J Biol Chem. 2007 Feb 23;282(8):5296-301. doi: 10.1074/jbc.M609343200. Epub 2006 Dec 21.
Pubmed: 17189259
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Pubmed: 14702039
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Pubmed: 18342636
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Pubmed: 11984834
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Pubmed: 14654938
Andrulis IL, Chen J, Ray PN: Isolation of human cDNAs for asparagine synthetase and expression in Jensen rat sarcoma cells. Mol Cell Biol. 1987 Jul;7(7):2435-43. doi: 10.1128/mcb.7.7.2435.
Pubmed: 2886907
Zhang YP, Lambert MA, Cairney AE, Wills D, Ray PN, Andrulis IL: Molecular structure of the human asparagine synthetase gene. Genomics. 1989 Apr;4(3):259-65.
Pubmed: 2565875
Suchi M, Sano H, Mizuno H, Wada Y: Molecular cloning and structural characterization of the human histidase gene (HAL). Genomics. 1995 Sep 1;29(1):98-104. doi: 10.1006/geno.1995.1219.
Pubmed: 8530107
Suchi M, Harada N, Wada Y, Takagi Y: Molecular cloning of a cDNA encoding human histidase. Biochim Biophys Acta. 1993 Nov 16;1216(2):293-5. doi: 10.1016/0167-4781(93)90157-9.
Pubmed: 7916645
Finckh U, Kohlschutter A, Schafer H, Sperhake K, Colombo JP, Gal A: Prenatal diagnosis of carbamoyl phosphate synthetase I deficiency by identification of a missense mutation in CPS1. Hum Mutat. 1998;12(3):206-11. doi: 10.1002/(SICI)1098-1004(1998)12:3<206::AID-HUMU8>3.0.CO;2-E.
Pubmed: 9711878
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Pubmed: 12955727
Aoshima T, Kajita M, Sekido Y, Kikuchi S, Yasuda I, Saheki T, Watanabe K, Shimokata K, Niwa T: Novel mutations (H337R and 238-362del) in the CPS1 gene cause carbamoyl phosphate synthetase I deficiency. Hum Hered. 2001;52(2):99-101. doi: 10.1159/000053360.
Pubmed: 11474210
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Nakatani Y, Banner C, von Herrath M, Schneider ME, Smith HH, Freese E: Comparison of human brain and liver glutamate dehydrogenase cDNAS. Biochem Biophys Res Commun. 1987 Dec 16;149(2):405-10. doi: 10.1016/0006-291x(87)90381-0.
Pubmed: 3426581
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Pubmed: 3377777
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Hayasaka K, Nanao K, Takada G, Okamura-Ikeda K, Motokawa Y: Isolation and sequence determination of cDNA encoding human T-protein of the glycine cleavage system. Biochem Biophys Res Commun. 1993 Apr 30;192(2):766-71. doi: 10.1006/bbrc.1993.1480.
Pubmed: 7916605
Nanao K, Takada G, Takahashi E, Seki N, Komatsu Y, Okamura-Ikeda K, Motokawa Y, Hayasaka K: Structure and chromosomal localization of the aminomethyltransferase gene (AMT) Genomics. 1994 Jan 1;19(1):27-30.
Pubmed: 8188235
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