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At least 19 recordsLinked to original sources
PubMed1975

Alpha-methyl-L-glutamic acid uptake by high affinity dicarboxylic amino acid transport system in Streptococcus faecalis.

The transport of alpha-methyl-L-glutamic acid was studied in Streptococcus faecalis. Energey-dependent uptake against substantial concentration gradients was observed. Kinetic experiments indicated that, in contrast to L-glutamic acid, only a single catalytic component (high affinity) and a diffusion controlled process participated in alpha-methyl-L-glutamic acid uptake. At concentrations up to 10 mM, alpha-methyl-glutamate transport was almost completely abolished in a mutant strain lacking a high affinity dicarboxylic amino acid transport system. In competition experiments, alpha-methylglutamic acid antagonized glutamate uptake via the high affinity system, and only slightly via the low affinity system. Column chromatography of cell extracts showed that very little (approx. 5%) of the accumulated amino acid was converted to metabolites during short term incubations. These studies indicate that, at concentrations up to 3-5 mM, alpha-methyl-L-glutamic acid can be used as a specific, relatively metabolically inert substrate of the high affinity dicarboxylic amino acid transport system in S. faecalis.

Amino Acids, Dicarboxylic↗
PubMed2004

Coordination modes vs. antitumor activity: synthesis and antitumor activity of novel platinum(II) complexes of N-substituted amino dicarboxylic acids.

The trans-(+/-)-1,2-diaminocyclohexaneplatinum(II) complexes of multidentate L-glutamate (Glu) and L-aspartate (Asp) were prepared and their antitumor activity was examined in relation with their coordination modes. All these complexes were obtained as a mixture of (O,O')- and (O,N)-chelate isomers due to rapid isomerization of the initially formed (O,O')-isomer to the thermodynamically more stable (O,N)-isomer. The (O,O')/(O,N)-isomeric mixture with the mole ratio of 80/20 exhibited excellent antitumor activity while the pure (O,N)-isomer was only marginally active. Therefore, in order to prevent the linkage isomerization of the active (O,O')-isomer to the inactive (O,N)-isomer, we have designed N-substituted amino dicarboxylic acids as a leaving group and prepared a new series of complexes, [Pt(dach)(RGlu)] and [Pt(dach)(RAsp)] (dach=trans-(+/-)-1,2-diaminocyclohexane; R=acetyl (Ac), propionyl (Pro), pivaloyl (Piv), carbobenzyloxy (Cbz) or phthaloyl (Phth)) and characterized by means of elemental analyses, and 1H NMR, 195Pt NMR and IR spectroscopies. The N-substituted amino dicarboxylate ligands were found to coordinate to platinum(II) ion through only the (O,O')-chelation mode, and their Pt(II) complexes were chemically stable in aqueous solution. The present Pt(II) complexes of N-substituted amino dicarboxylic acids showed excellent antitumor activity against both murine leukemia L1210 and human tumor cells. Especially, the highly hydrophobic N-phthaloylglutamate complex, [Pt(dach)(PhthGlu)], exhibited an outstanding in vitro activity (IC50=2.22 microM) on the human stomach cancer cells which are not responsive to cisplatin and carboplatin.

Amino Acids, Dicarboxylic↗
PubMed1999

Conversion of tyrosine phenol-lyase to dicarboxylic amino acid beta-lyase, an enzyme not found in nature.

Tyrosine phenol-lyase (TPL), which catalyzes the beta-elimination reaction of L-tyrosine, and aspartate aminotransferase (AspAT), which catalyzes the reversible transfer of an amino group from dicarboxylic amino acids to oxo acids, both belong to the alpha-family of vitamin B6-dependent enzymes. To switch the substrate specificity of TPL from L-tyrosine to dicarboxylic amino acids, two amino acid residues of AspAT, thought to be important for the recognition of dicarboxylic substrates, were grafted into the active site of TPL. Homology modeling and molecular dynamics identified Val-283 in TPL to match Arg-292 in AspAT, which binds the distal carboxylate group of substrates and is conserved among all known AspATs. Arg-100 in TPL was found to correspond to Thr-109 in AspAT, which interacts with the phosphate group of the coenzyme. The double mutation R100T/V283R of TPL increased the beta-elimination activity toward dicarboxylic amino acids at least 10(4)-fold. Dicarboxylic amino acids (L-aspartate, L-glutamate, and L-2-aminoadipate) were degraded to pyruvate, ammonia, and the respective monocarboxylic acids, e.g. formate in the case of L-aspartate. The activity toward L-aspartate (kcat = 0.21 s-1) was two times higher than that toward L-tyrosine. beta-Elimination and transamination as a minor side reaction (kcat = 0.001 s-1) were the only reactions observed. Thus, TPL R100T/V283R accepts dicarboxylic amino acids as substrates without significant change in its reaction specificity. Dicarboxylic amino acid beta-lyase is an enzyme not found in nature.

Amino Acid Sequence↗
PubMed1981

Prevention of insulin aggregation by dicarboxylic amino acids during prolonged infusion.

The dicarboxylic amino acids, aspartic and glutamic acid, at their isoelectric pH, reduced aggregation of insulin solutions in vitro for 16 days during continuous agitation at 37 degrees C. Unprotected insulin solutions, when infused via a 14-day implantable infusion device in diabetic Chinese hamsters, controlled plasma glucose levels for only 2 days, followed by escape coincident with insulin aggregation. However, when insulin solutions were protected with glutamic acid, euglycemia was maintained for the 14-day life of the device.

Animals↗
PubMedDate not supplied

[Effects of parenterally administered dicarboxylic amino acids and their amides on the secretory function of the stomach].

The effect of dicarboxylic amino acids and their amides on gastric secretion stimulated by sham-feeding (100 g of raw meat), as well as of amides of dicarboxylic amino acids on the gastric secretory function was studied in 119 tests on 8 dogs with gastric fistulas according to Basov. The tests were started 16-18 h after feeding under neutral or alkaline reactions of gastric excretion. The tests demonstrated that dicarboxylic amino acids inhibited gastric secretion induced by sham-feeding. It was shown that dicarboxylic amino acid amines, in contrast to these amino acids, did not inhibit gastric secretion induced by sham-feeding. On the contrary, asparagine and glutamine administered into the blood are capable of inducing gastric secretion, per se.

Alanine↗
PubMed1979

Dicarboxylic amino acid uptake in normal, Friedreich's ataxia, and dicarboxylic aminoaciduria fibroblasts.

Glutamic and aspartic acid uptake was measured in skin fibroblasts from patients with Friedreich's Ataxia, dicarboxylic aminoaciduria, and normal individuals. The results showed no difference in uptake kinetics of either dicarboxylic amino acids between Friedreich's Ataxia and normal cells, but reduced uptake velocities in dicarboxylic aminoaciduria fibroblasts. Friedreich's Ataxia fibroblasts were, however, less calcium-dependent and more magnesium and phosphate-dependent than controls in glucose-free incubation mixture. This difference might be related to some degree of glucose intolerance by Friedreich's Ataxia fibroblasts in culture.

Amino Acids↗
PubMedDate not supplied

[Inhibitory effect of parenterally administered dicarboxylic amino acids on gastric secretion].

Tests conducted on dogs established that glutaminic and aspargic acids introduced into the blood by the drip method call forth inhibition of the gastric secretion stimulated by other amino acids (alanine, glycine, proline). The dicarboxylic amino acids inhibit also the reflex phase of the gastric secretion provoked by injection of histamine. It is only against the background of a repeated introduction of histamine for many hours that they produce a sharply marked inhibitory effect. This manifests itself chiefly in dogs with denervated isolated pouches, while with intact innervation of gastric glands this effect is very poorly pronounced. Introduction of beta-adrenolytic-obsidan is attended by a drastic reduction of this effect.

Animals↗
PubMed1981

Uptake of 14C-labeled dicarboxylic amino acids in hepatocytes and hepatoma cells.

In previous studies, we observed decreased uptake of 14C-labeled L-aspartate and L-glutamate in s.c. transplants of several rapidly growing hepatomas relative to that in normal liver. The present report extends these observations to isolated cells and indicates that circulation differences cannot be the major factor. Mean net uptakes for the two dicarboxylic amino acids in cells from the rapidly growing Morris Hepatomas 7288ctc and 7777 were 5 to 26% of corresponding values for normal hepatocytes. Rates for net uptake in Hepatoma 7787 cells were intermediate between those of the rapidly growing hepatomas and hepatocytes, while the rates for Hepatoma 5123C cells and hepatocytes were similar. The contribution of sodium-dependent uptake to the mean total net uptake of [14C]aspartate and [14C]glutamate tended to be higher in hepatoma cells than in hepatocytes. Studies with isolated hepatocytes and Hepatoma 5123C cells showed no significant effect on uptake by 10 mM alpha-(methylamino)isobutyric acid and 10 mM 2-amino-2-carboxybicyclo[2.2.1]heptane. On the other hand, L-cysteic acid, L-alanosine, and N-phosphonacetyl-L-aspartic acid were shown to be effective inhibitors of sodium-dependent uptake in Hepatoma 5123C cells. The data suggest that the A and L systems are not major contributors to the uptake of dicarboxylic amino acids in hepatic cells. It was concluded that decreased uptake of dicarboxylic amino acids in rapidly growing hepatomas may accompany decreased metabolism of these dietary nonessential amino acids.

Alanine↗
PubMed1982

[Metabolism of dicarboxylic amino acids and their amides in bacteria of the genus Klebsiella].

The pathways of the utilization of dicarboxylic amino acids and their amides in 55 Klebsiella strains have been studied. These organisms have been found to be capable of carboxylating glutaminic acid with the subsequent utilization of the product of this reaction, gamma-amino butyric acid, by reamidization with alpha-glutaric acid. Aspartate decarboxylase with low activity has been detected only in a small number of strains. Most of the strains have been shown to be capable of deamidizating equally asparaginic and glutaminic acids. The presence of active asparaginase and glutaminase has been detected in a considerable number of these strains. Microorganisms of the genus Klebsiella have low asparagine synthetase and glutamine synthetase activity. Aspartate aminotransferase has been found to occur twice as frequently as alanine aminotransferase, both having the same level of activity.

Amides↗