Title : Inversion of allosteric effect of arginine on N-acetylglutamate synthase, a molecular marker for evolution of tetrapods.

Pub. Date : 2008 Sep 18

PMID : 18801197






17 Functional Relationships(s)
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1 Inversion of allosteric effect of arginine on N-acetylglutamate synthase, a molecular marker for evolution of tetrapods. Arginine N-acetylglutamate synthase Homo sapiens
2 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 N-acetylglutamate synthase Homo sapiens
3 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 N-acetylglutamate synthase Homo sapiens
4 Arginine is an allosteric inhibitor of microbial and plant NAGS, and allosteric activator of mammalian NAGS. Arginine N-acetylglutamate synthase Homo sapiens
5 Arginine is an allosteric inhibitor of microbial and plant NAGS, and allosteric activator of mammalian NAGS. Arginine N-acetylglutamate synthase Homo sapiens
6 RESULTS: Information from mutagenesis studies of E. coli and P. aeruginosa NAGS was combined with structural information from the related bacterial N-acetylglutamate kinases to identify four residues in mammalian NAGS that interact with arginine. Arginine N-acetylglutamate synthase Homo sapiens
7 Substitutions of these four residues were engineered in mouse NAGS and into the vertebrate-like N-acetylglutamate synthase-kinase (NAGS-K) of Xanthomonas campestris, which is inhibited by arginine. Arginine N-acetylglutamate synthase Homo sapiens
8 Substitutions of these four residues were engineered in mouse NAGS and into the vertebrate-like N-acetylglutamate synthase-kinase (NAGS-K) of Xanthomonas campestris, which is inhibited by arginine. Arginine N-acetylglutamate synthase Homo sapiens
9 Fish NAGS were partially inhibited by arginine and frog NAGS were activated by arginine. Arginine N-acetylglutamate synthase Homo sapiens
10 Fish NAGS were partially inhibited by arginine and frog NAGS were activated by arginine. Arginine N-acetylglutamate synthase Homo sapiens
11 Fish NAGS were partially inhibited by arginine and frog NAGS were activated by arginine. Arginine N-acetylglutamate synthase Homo sapiens
12 CONCLUSION: Difference in arginine effect on bacterial and mammalian NAGS most likely stems from the difference in the type of conformational change triggered by arginine binding to these proteins. Arginine N-acetylglutamate synthase Homo sapiens
13 CONCLUSION: Difference in arginine effect on bacterial and mammalian NAGS most likely stems from the difference in the type of conformational change triggered by arginine binding to these proteins. Arginine N-acetylglutamate synthase Homo sapiens
14 The change from arginine inhibition of NAGS to activation was gradual, from complete inhibition of bacterial NAGS, to partial inhibition of fish NAGS, to activation of frog and mammalian NAGS. Arginine N-acetylglutamate synthase Homo sapiens
15 The change from arginine inhibition of NAGS to activation was gradual, from complete inhibition of bacterial NAGS, to partial inhibition of fish NAGS, to activation of frog and mammalian NAGS. Arginine N-acetylglutamate synthase Homo sapiens
16 The change from arginine inhibition of NAGS to activation was gradual, from complete inhibition of bacterial NAGS, to partial inhibition of fish NAGS, to activation of frog and mammalian NAGS. Arginine N-acetylglutamate synthase Homo sapiens
17 The change from arginine inhibition of NAGS to activation was gradual, from complete inhibition of bacterial NAGS, to partial inhibition of fish NAGS, to activation of frog and mammalian NAGS. Arginine N-acetylglutamate synthase Homo sapiens