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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Reaction
Reaction on EC 2.7.2.8 - acetylglutamate kinase
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ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate
mechanism
ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate
random bi-bi mechanism
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ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate
enzyme has to interact stoichiometrically with acetylglutamate synthase in order to be active
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ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate
using an elastic network model representation a normal mode analysis shows that the conformational mechanisms for substrate binding by NAGK strongly correlate with the intrinsic dynamics of the enzyme in the unbound form. The conformational change observed between the open and closed forms of EcNAGK are essentially accomplished by movements along a small subset of modes
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ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate
allosterically regulated mechanism for the enzyme from Maricaulis maris with roles for Lys356, Arg386, Asn391 and Tyr397 in the catalytic mechanism
ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate
allosterically regulated mechanism for the enzyme from Maricaulis maris with roles for Lys356, Arg386, Asn391 and Tyr397 in the catalytic mechanism
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