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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General Information
General Information on EC 2.7.2.8 - acetylglutamate kinase
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evolution
malfunction
metabolism
physiological function
the allosterically regulated mechanism for mmNAGS/K differs significantly from that for Neisseria gonorrhoeae NAGS. L-Arginine is an allosteric inhibitor of NAGS/K but an allosteric activator of mammalian NAGS
evolution
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the allosterically regulated mechanism for mmNAGS/K differs significantly from that for Neisseria gonorrhoeae NAGS. L-Arginine is an allosteric inhibitor of NAGS/K but an allosteric activator of mammalian NAGS
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argB gene coding the N-acetyl-L-glutamate kinase is first overexpressed in the strain SYPA5-5, whereas the L-arginine production is narrowly increased by 15.4%
malfunction
enzyme mutations lower pollen tube competitiveness. Mutant pollen tubes grow more slowly than wild type pollen tubes. Mutant female gametophytes are defective in micropylar pollen tube guidance. Loss-of-function of enzyme results in Arabidopsis embryos not developing beyond the four-celled embryo stage
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Sulfolobus solfataricus lacks ornithine acetyltransferase and thus forms N-acetylglutamate exclusively via the energetically less favourable reaction catalysed by N-acetylglutamate synthase, investing 1 mol of acetyl CoA per mol of N-acetyl intermediate synthesized
metabolism
N-acetylglutamate synthase/kinase catalyzes a rate limiting step in L-arginine biosynthesis. The activity of the enzyme is allosterically regulated by L-arginine, The pathway and regulatory modes involved in l-arginine biosynthesis in Corynebacterium crenatum SYPA5-5, overview
metabolism
N-acetylglutamate synthase/kinase catalyzes the first two steps in L-arginine biosynthesis
metabolism
N-acetylglutamate synthase/kinase catalyzes the first two steps in L-arginine biosynthesis. The synthase activity of mmNAGS/K is allosterically regulated by L-arginine
metabolism
the enzyme catalyzes the second step of arginine biosynthesis
metabolism
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N-acetylglutamate synthase/kinase catalyzes a rate limiting step in L-arginine biosynthesis. The activity of the enzyme is allosterically regulated by L-arginine, The pathway and regulatory modes involved in l-arginine biosynthesis in Corynebacterium crenatum SYPA5-5, overview
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metabolism
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N-acetylglutamate synthase/kinase catalyzes the first two steps in L-arginine biosynthesis. The synthase activity of mmNAGS/K is allosterically regulated by L-arginine
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metabolism
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N-acetylglutamate synthase/kinase catalyzes the first two steps in L-arginine biosynthesis
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the enzyme is required for both gametophyte function and embryo development
physiological function
the enzyme plays a vital role in enhancing drought tolerance by likely affecting the arginine and nitric oxide accumulation. The enzyme is involved in different strategies in response to drought stress. The ectopic expression of the maize enzyme in tobacco results in higher tolerance to drought compared to plants transformed with empty vector. Enzyme overexpression can enhance the activities of antioxidant defense enzymes, and decrease malondialdehyde content and leakage of electrolyte in tobacco under drought stress. Moreover, the transgenic tobacco accumulate more arginine and nitric oxide than control plants under drought stress