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10.3390/ijms160613004 http://scihub22266oqcxt.onion/10.3390/ijms160613004 C4490483!4490483!26068232     free     free     free Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Int+J+Mol+Sci 2015 ; 16 (6): 13004-22 Nephropedia Template TP {{tp|p=26068232|t=2015. The N-Acetylglutamate Synthase Family: Structures, Function and Mechanisms |pdf=|usr=}}{{26068232}} gab.com Text The N-Acetylglutamate Synthase Family: Structures, Function and Mechanisms JO: Int J Mol Sci http://www.kidney.de/pget.php?&tw=1&pmid=26068232 #FOAvip N-acetylglutamate synthase (NAGS) catalyzes the production of N-acetylglutamate (NAG) from acetyl-CoA and l-glutamate. In microorganisms and plants, the enzyme functions in the arginine biosynthetic pathway, while in mammals, its major role is to produce the essential co-factor of carbamoyl phosphate synthetase 1 (CPS1) in the urea cycle. Recent work has shown that several different genes encode enzymes that can catalyze NAG formation. A bifunctional enzyme was identified in certain bacteria, which catalyzes both NAGS and N-acetylglutamate kinase (NAGK) activities, the first two steps of the arginine biosynthetic pathway. Interestingly, these bifunctional enzymes have higher sequence similarity to vertebrate NAGS than those of the classical (mono-functional) bacterial NAGS. Solving the structures for both classical bacterial NAGS and bifunctional vertebrate-like NAGS/K has advanced our insight into the regulation and catalytic mechanisms of NAGS, and the evolutionary relationship between the two NAGS groups. Twit Text FOAVip The N-Acetylglutamate Synthase Family: Structures, Function and Mechanisms ????Int J Mol Sci http://www.kidney.de/pget.php?&tw=1&pmid=26068232 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26068232 #FOAvip English Wikipedia <ref>{{Cite pmid|26068232}}</ref> The N-Acetylglutamate Synthase Family: Structures, Function and Mechanisms #MMPMID26068232 Shi D; Allewell NM; Tuchman M Int J Mol Sci 2015[Jun]; 16 (6): 13004-22 PMID26068232show ga N-acetylglutamate synthase (NAGS) catalyzes the production of N-acetylglutamate (NAG) from acetyl-CoA and l-glutamate. In microorganisms and plants, the enzyme functions in the arginine biosynthetic pathway, while in mammals, its major role is to produce the essential co-factor of carbamoyl phosphate synthetase 1 (CPS1) in the urea cycle. Recent work has shown that several different genes encode enzymes that can catalyze NAG formation. A bifunctional enzyme was identified in certain bacteria, which catalyzes both NAGS and N-acetylglutamate kinase (NAGK) activities, the first two steps of the arginine biosynthetic pathway. Interestingly, these bifunctional enzymes have higher sequence similarity to vertebrate NAGS than those of the classical (mono-functional) bacterial NAGS. Solving the structures for both classical bacterial NAGS and bifunctional vertebrate-like NAGS/K has advanced our insight into the regulation and catalytic mechanisms of NAGS, and the evolutionary relationship between the two NAGS groups. äThe N-Acetylglutamate Synthase Family: Structures, Function and Mechan(epmc).pdf DeepDyve Pubget Overpricing