2.7.2.8: acetylglutamate kinase
This is an abbreviated version!
For detailed information about acetylglutamate kinase, go to the full flat file.
Reaction
Synonyms
acetylglutamate kinase, acetylglutamate phosphokinase, amino-acid acetyltransferase, argB, CcNAGK, EcNAGK, GRMZM2G132777, kinase, acetylglutamate (phosphorylating), mmNAGS/K, N-acetyl glutamate kinase, N-acetyl-glutamate 5-phosphotransferase, N-acetyl-L-glutamate 5-phosphotransferase, N-acetyl-L-glutamate kinase, N-acetyl-L-glutamate synthase/kinase, N-acetylglutamate 5-phosphotransferase, N-acetylglutamate kinase, N-acetylglutamate phosphokinase, N-acetylglutamate-5-phosphotransferase, N-acetylglutamic 5-phosphotransferase, NagK, NAGK1, NAGS-K, SYPA5-5 N-acetylglutamate kinase, xcNAGS/K, yNAGK
ECTree
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Inhibitors
Inhibitors on EC 2.7.2.8 - acetylglutamate kinase
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arginine
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enzyme has no allosteric properties and its activity is influenced neither by arginine nor by any of the intermediates of the arginine biosynthetic pathway
arginine
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feedback inhibition is markedly dependent on pH, above pH 9 no inhibition
arginine
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feedback inhibition is markedly dependent on pH, above pH 9 no inhibition
arginine
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feedback regulation of enzyme and N-acetylglutamate synthase is mutually interdependent, enzymes form a complex
L-arginine
complete inhibition at 3-5 mM, PII-mediated relief from L-arginine inhibition is antagonized by 2-oxoglutarate
L-arginine
feedback inhibition. SYPA5-5 N-acetylglutamate kinase feedback inhibition by L-arginine can be deregulated by introducing point mutations, H268N or R209A
L-arginine
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feedback inhibition, almost complete inhibition at 10 mM
L-arginine
an allosteric inhibitor of mmNAGS/K, mechanism of allosteric inhibition of mmNAGS/K by L-arginine. L-Arginine is an allosteric inhibitor of NAGS/K but an allosteric activator of mammalian NAGS. In contrast to the structure of mmNAGS/K in the absence of L-arginine where there are conformational differences between the four subunits in the asymmetric unit, all four subunits in the L-arginine liganded structure have very similar conformations. In this conformation, the AcCoA binding site in the N-acetyltransferase domain is blocked by a loop from the amino acid kinase domain, as a result of a domain rotation that occurs when L-arginine binds
L-arginine
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sigmoidal arginine inhibition kinetics, feedback inhibition, indentification of the N-terminal arginine site, mutational analysis, the mobile alphaH-beta16 loop of the arginine site is the modulatory signal receiver, overview
L-arginine
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wild type enzyme activity drastically decreases by addition of 0.2 mM L-Arg, and consequently decreases when L-Arg concentration is increased, indicating that the enzyme activity is subject to feedback inhibition by L-Arg. Enzyme activity is almost lost in the presence of 1.0 mM L-Arg
L-arginine
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complete inhibition at 0.1-1.0 mM, PII-mediated relief from L-arginine inhibition is antagonized by 2-oxoglutarate
L-arginine
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pH and temperature dependent, sigmoidal dependence on concentration of arginine, Hill coefficient of 4, 1 mM, 37°C, 95% inhibition
additional information
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not inhibitory: D-arginine, agmatine, citrulline, L-canavanine, L-lysine, L-ornithine, guanidinium ions, urea at 1 mM, 37°C
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