Title |
Inversion of allosteric effect of arginine on N-acetylglutamate synthase, a molecular marker for evolution of tetrapods
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Published in |
BMC Molecular and Cell Biology, September 2008
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DOI | 10.1186/1471-2091-9-24 |
Pubmed ID | |
Authors |
Nantaporn Haskins, Maria Panglao, Qiuhao Qu, Himani Majumdar, Juan Cabrera-Luque, Hiroki Morizono, Mendel Tuchman, Ljubica Caldovic |
Abstract |
The efficient conversion of ammonia, a potent neurotoxin, into non-toxic metabolites was an essential adaptation that allowed animals to move from the aquatic to terrestrial biosphere. The urea cycle converts ammonia into urea in mammals, amphibians, turtles, snails, worms and many aquatic animals and requires N-acetylglutamate (NAG), an essential allosteric activator of carbamylphosphate synthetase I (CPSI) in mammals and amphibians, and carbamylphosphate synthetase III (CPSIII) in fish and invertebrates. NAG-dependent CPSI and CPSIII catalyze the formation of carbamylphosphate in the first and rate limiting step of ureagenesis. NAG is produced enzymatically by N-acetylglutamate synthase (NAGS), which is also found in bacteria and plants as the first enzyme of arginine biosynthesis. Arginine is an allosteric inhibitor of microbial and plant NAGS, and allosteric activator of mammalian NAGS. |
Mendeley readers
Geographical breakdown
Country | Count | As % |
---|---|---|
United States | 1 | 4% |
Unknown | 27 | 96% |
Demographic breakdown
Readers by professional status | Count | As % |
---|---|---|
Student > Ph. D. Student | 9 | 32% |
Student > Bachelor | 4 | 14% |
Professor > Associate Professor | 3 | 11% |
Student > Master | 3 | 11% |
Researcher | 2 | 7% |
Other | 5 | 18% |
Unknown | 2 | 7% |
Readers by discipline | Count | As % |
---|---|---|
Agricultural and Biological Sciences | 13 | 46% |
Biochemistry, Genetics and Molecular Biology | 4 | 14% |
Veterinary Science and Veterinary Medicine | 2 | 7% |
Medicine and Dentistry | 2 | 7% |
Social Sciences | 1 | 4% |
Other | 3 | 11% |
Unknown | 3 | 11% |