Disease relevance of N-acetylglutamic acid

• N-Acetylglutamic acid: an extracellular nod signal of Rhizobium trifolii ANU843 that induces root hair branching and nodule-like primordia in white clover roots [1].
• Complex formation and catalytic activation by the PII signaling protein of N-acetyl-L-glutamate kinase from Synechococcus elongatus strain PCC 7942 [2].
• Some kinetic properties of N-acetylglutamate 5-phosphotransferase (ATP: N-acetyl-L-glutamate 5-phosphotransferase EC 2.7.2.8) purified approx. 2000-fold from Pseudomonas aeruginosa have been studied [3].
• N-Acetyl-L-glutamate kinase from Escherichia coli: cloning of the gene, purification and crystallization of the recombinant enzyme and preliminary X-ray analysis of the free and ligand-bound forms [4].
• Partial N-acetyl-glutamate synthetase deficiency masquerading as a valproic acid-induced Reye-like syndrome [5].

Psychiatry related information on N-acetylglutamic acid

• Intraventricular N-acetyl-L-glutamate induces retrograde amnesia in chicks [6].

High impact information on N-acetylglutamic acid

• Enzyme kinetic analysis showed that PII increases N-acetyl glutamate kinase activity slightly, but the primary function of binding is to relieve inhibition of enzyme activity by the pathway product, arginine [7].
• The interaction of PII with N-acetyl glutamate kinase was confirmed through pull-down, gel filtration, and isothermal titration calorimetry experiments, and binding was shown to be enhanced in the presence of the downstream product, arginine [7].
• These results indicate that extracellular accumulation of N-acetylglutamic acid is linked to flavone-dependent metabolism involving nodD, nodL, and nodM in R. trifolii ANU843 [1].
• Purification of N-acetyl-L-glutamate synthetase from rat liver mitochondria and substrate and activator specificity of the enzyme [8].
• Purification and properties of the glutamine- and N-acetyl-L-glutamate-dependent carbamoyl phosphate synthetase from liver of Squalus acanthias [9].

Chemical compound and disease context of N-acetylglutamic acid

• N-Acetylglutamate 5-phosphotransferase (ATP: N-acetyl-L-glutamate 5-phosphotransferase EC 2.7.2.8), the second enzyme of arginine biosynthesis, was purified over 2000-fold from Pseudomonas aeruginosa [10].

Biological context of N-acetylglutamic acid

• The PII signal transduction protein of Arabidopsis thaliana forms an arginine-regulated complex with plastid N-acetyl glutamate kinase [7].
• N-Acetyl-L-glutamate kinase (NAGK), the structural paradigm of the enzymes of the amino acid kinase family, catalyzes the phosphorylation of the gamma-COO(-) group of N-acetyl-L-glutamate (NAG) by ATP [11].
• Carbamoyl-phosphate synthetase was inactivated by elastase with first-order kinetics, and N-acetyl-L-glutamate speeded inactivation [12].
• The substrate specificity was narrow: N-carbamoyl-L-glutamate and N-formyl-L-glutamate were phosphorylated, but at a lower rate than N-acetyl-L-glutamate; N-propionyl-L-glutamate was almost inactive as a substrate. dATP, but neither GTP nor ITP, could be used instead of ATP [3].

Anatomical context of N-acetylglutamic acid

• When mitochondria from fasted rats were incubated at 25 degrees C, about 40% of N-acetyl-L-glutamate passed from the mitochondria to the medium in 60 min [13].
• The observations, together with previous results, indicate that N-acetyl-L-glutamate degradation is positively regulated by a modification of its efflux through mitochondrial membranes [13].
• Since AG levels change under a number of conditions, we checked for an AG deacylase in mitochondria, for otherwise AG must be exported and destroyed by cytosol deacylases [14].

Associations of N-acetylglutamic acid with other chemical compounds

• The major PII-interacting protein is the chloroplast-localized enzyme N-acetyl glutamate kinase, which catalyzes the key regulatory step in the pathway to arginine biosynthesis [7].
• N-Acetyl-L-glutamate (N-acetylglutamate) content and N-acetylglutamate synthase activity ranges were established in human liver tissue homogenates by stable isotope dilution [15].
• The positive allosteric cofactor N-acetyl-L-glutamate (AGA) is required for CPSase I activity and is important for regulation of the urea cycle [16].

Gene context of N-acetylglutamic acid

• All enzyme levels were normal except N-acetyl glutamate-dependent carbamyl phosphate synthetase 1 (CPS1) which was half the mean activity in normal control specimens [17].
• N-Acetyl-L-glutamate synthetase catalyzes the synthesis of N-acetyl-L-glutamate, an allosteric and essential activator of carbamoyl-phosphate synthetase I in the liver of ureotelic animals [18].
• Carbamate kinase from Enterococcus faecalis and Enterococcus faecium--cloning of the genes, studies on the enzyme expressed in Escherichia coli, and sequence similarity with N-acetyl-L-glutamate kinase [19].
• Acute glucagon treatment in rats fed various protein diets effect on n-acetyl glutamate concentration [20].

Analytical, diagnostic and therapeutic context of N-acetylglutamic acid

• An extracellular metabolite purified from Rhizobium trifolii ANU843 was established as N-acetylglutamic acid (GluNAc) by 1H NMR and Fourier transform IR spectroscopy, gas chromatography/mass spectrometry of its methylated product, and organic synthesis [1].
• Determination of N-acetyl-L-glutamate using high-performance liquid chromatography [21].
• A significant increase in N-acetyl-L-glutamate concentration in rat liver on hypophysectomy and its reversal back to normal levels on growth hormone administration was reported [22].
• N-Acetyl-L-glutamate (NAG), the activator of mitochondrial carbamoyl phosphate synthetase (CPS), is demonstrated by several methods, including a new HPLC assay, in the brain of mammals and of chicken [23].

References