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10.1038/srep16950 http://scihub22266oqcxt.onion/10.1038/srep16950 C4655335!4655335 !26592762     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=26592762 &cmd=llinks): Failed to open stream: HTTP request failed! 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Structure of human carbamoyl phosphate synthetase: deciphering the on/off switch of human ureagenesis |pdf=|usr=}}{{26592762 }} gab.com Text Structure of human carbamoyl phosphate synthetase: deciphering the on/off switch of human ureagenesis JO: Sci Rep http://www.kidney.de/pget.php?&tw=1&pmid=26592762 #FOAvip Human carbamoyl phosphate synthetase (CPS1), a 1500-residue multidomain enzyme, catalyzes the first step of ammonia detoxification to urea requiring N-acetyl-L-glutamate (NAG) as essential activator to prevent ammonia/amino acids depletion. Here we present the crystal structures of CPS1 in the absence and in the presence of NAG, clarifying the on/off-switching of the urea cycle by NAG. By binding at the C-terminal domain of CPS1, NAG triggers long-range conformational changes affecting the two distant phosphorylation domains. These changes, concerted with the binding of nucleotides, result in a dramatic remodeling that stabilizes the catalytically competent conformation and the building of the ~35?Å-long tunnel that allows migration of the carbamate intermediate from its site of formation to the second phosphorylation site, where carbamoyl phosphate is produced. These structures allow rationalizing the effects of mutations found in patients with CPS1 deficiency (presenting hyperammonemia, mental retardation and even death), as exemplified here for some mutations. Twit Text FOAVip Structure of human carbamoyl phosphate synthetase: deciphering the on/off switch of human ureagenesis ????Sci Rep http://www.kidney.de/pget.php?&tw=1&pmid=26592762 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26592762 #FOAvip English Wikipedia <ref>{{Cite pmid|26592762 }}</ref> Structure of human carbamoyl phosphate synthetase: deciphering the on/off switch of human ureagenesis #MMPMID26592762 de Cima S ; Polo LM ; Díez-Fernández C ; Martínez AI ; Cervera J ; Fita I ; Rubio V Sci Rep 2015[Nov]; 5 (ä): 16950 PMID26592762 show ga Human carbamoyl phosphate synthetase (CPS1), a 1500-residue multidomain enzyme, catalyzes the first step of ammonia detoxification to urea requiring N-acetyl-L-glutamate (NAG) as essential activator to prevent ammonia/amino acids depletion. Here we present the crystal structures of CPS1 in the absence and in the presence of NAG, clarifying the on/off-switching of the urea cycle by NAG. By binding at the C-terminal domain of CPS1, NAG triggers long-range conformational changes affecting the two distant phosphorylation domains. These changes, concerted with the binding of nucleotides, result in a dramatic remodeling that stabilizes the catalytically competent conformation and the building of the ~35?Å-long tunnel that allows migration of the carbamate intermediate from its site of formation to the second phosphorylation site, where carbamoyl phosphate is produced. These structures allow rationalizing the effects of mutations found in patients with CPS1 deficiency (presenting hyperammonemia, mental retardation and even death), as exemplified here for some mutations. |Amino Acid Motifs [MESH] |Ammonia/*chemistry/metabolism [MESH] |Animals [MESH] |Baculoviridae/genetics/metabolism [MESH] |Carbamoyl-Phosphate Synthase (Ammonia)/*chemistry/genetics/metabolism [MESH] |Carbamoyl-Phosphate Synthase I Deficiency Disease/enzymology/genetics/pathology [MESH] |Carbamyl Phosphate/*chemistry/metabolism [MESH] |Cloning, Molecular [MESH] |Crystallography, X-Ray [MESH] |Gene Expression [MESH] |Glutamates/*chemistry/metabolism [MESH] |Humans [MESH] |Models, Molecular [MESH] |Molecular Sequence Data [MESH] |Mutation [MESH] |Phosphorylation [MESH] |Protein Structure, Secondary [MESH] |Protein Structure, Tertiary [MESH] |Recombinant Proteins/chemistry/genetics/metabolism [MESH] |Sf9 Cells [MESH] |Spodoptera [MESH] |Substrate Specificity [MESH]Structure of human carbamoyl phosphate synthetase: deciphering the on/(epmc).pdf DeepDyve Pubget Overpricing