Improved Synthesis of N-Alkyl-Aspartic Acids

Laliberté, Réal; Berlinguet, Louis

doi:10.1139/v62-027

Cited by 11 publications

(4 citation statements)

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“…Amphoteric derivatives of/3-alanine were prepared by the reaction of both primary and secondary amines and propiolactone as reported by Gresham, et al, (11). Piperidine and piperazine amphoterics also have been described (12,13).…”

Section: Introductionmentioning

confidence: 99%

Amphoteric surfactants from mixed N‐alkylethylenediamine

Bluestein¹,

Rosenblatt²,

Clark³

et al. 1973

J Americ Oil Chem Soc

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The preparation of amphoteric surfactants by the condensation of mixed N-alkylethylenediamines and unsaturated acid derivatives, particularly acrylic acid esters, was studied. The reaction proceeded readily near 100 C either neat or with solvents. Saponification of the ester products yielded salts which were water-soluble. The mono-and disodium salts of mixed N-alkyl (Cl1.5 av) ethylenediamine dipropionic and diisobutyric acid (crotonic acid derived) as 1% active in water were completely soluble at all pH levels. The solutions demonstrated no perceptible isoelectric range on addition of 1-10% concentrations of sodium chloride. Data on surface tension, solubility, calcium tolerance, foam, viscosity, color, and density are presented.

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Section: Introductionmentioning

confidence: 99%

Amphoteric surfactants from mixed N‐alkylethylenediamine

Bluestein¹,

Rosenblatt²,

Clark³

et al. 1973

J Americ Oil Chem Soc

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“…The most common synthetic route to N-substituted aspartic acids is through the direct Michael-type addition of amines to maleic acid, maleic anhydride, or the ester or amide derivatives of maleic acid. [5][6][7][8] Recently, a novel one-step method for the preparation of N-substituted aspartic acids from maleic anhydride and amines via the monolithium salt of maleic acid was reported. [9] However, the products of all these reactions were racemic mixtures, and further separation steps were needed to obtain an optically pure amino acid.…”

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confidence: 99%

Enantioselective Synthesis of N‐Substituted Aspartic Acids Using an Engineered Variant of Methylaspartate Ammonia Lyase

et al. 2013

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“…A preliminary report on this work has appeared (5). ), and N-allyl-DL-aspartic acid was prepared using the method of Lalibertk and Berlinguet (7). Male Sprague-Bawley rats between 150 and 400 g fed ad libitwn were sacrificed by decapitation and the livers were quickly removed.…”

mentioning

confidence: 99%

Inhibition of urea cycle enzymes by aspartic acid analogues

Bayer¹,

McMurray²

1969

Can. J. Biochem.

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BAYER, S. M., AND M c M m a a~, W. C. Inhibition of urea cycle enzymes by aspartic acid analogues. Can. J. Biochem. 47, 361-369 (1969).The inhibition of urea biosynthesis by anaIogues of aspartic acid was studied in vitro in homogenates and enzyme preparations from rat liver. Each of the analogues tested inhibited the overall utilization of citrulline for urea formation by liver homogenates. The concentrations required to give 50 % inhibition were: N-allylaspartate, 0.248 M ; a-methylaspartate, 0.140 M; 0-methylaspartate, 0.078 M ; and Bhydroxy-p-methyla~partate~ 6.038 M. The 0-substituted analogues partly replaced aspartate as a substrate for citrulline utilization in liver homogenates. The replacement was probably due to transamination of the analogues with oxaloacetate, since the effect was not observed when the assay mixture did not contain a substrate which could yield oxaloacetate.A study of individual enzymes of the urea cycle showed that arginase, argininosuccinase, and ormithine transcarbamylase were not greatly affected by the analogues. However, carbamyl phosphate synthetase as well as argininosuccinate synthetase were strongly inhibited, suggesting that the analogues act by some mechanism other than simple antagonism of aspartate. Part of the inhibition was related to the ability of the analogues to complex MgZ+, since increased concentrations of MgZ+ prevented the inhibition of carbamyl phosphate synthetase and reduced the inhibition of argininosuccinate synthekse by a-methylaspartate and N-alIylaspartate. In addition, I%-methylaspartate was found to depress oxidative and phosphorylative reactions, thus interfering with the energy production required for urea formation.Aspartic acid in concentrations comparable with those required to effect inhibition by a-methylaspartate produced a marked inhibition of citrulline utilization in liver homogenates and of purified argininosuccinate synthetase. This observation suggests that part of the inhibitions observed with the analogues are of the "substrate type"# a-Methylaspartic acid (I), p-methylaspartic acid (21, and Wallylaspartic acid (3) are reported to inhibit the synthesis of urea from citrulline and aspartic acid in rat liver homogenates. These analogues of aspartic acid are believed to act as antimetabolites of aspartic acid, and thus specifically inhibit argininosuccinate synthetase. This enzyme catalyzes the first reaction in the following sequence, leading to the synthesis of urea :Mg2 +[I ] citrulline + aspartic acid + ATB -----+ argininosuccinic acid + AMP + PP, [%I argininosuccinic acid -+ arginine + fumaric acid Mn2 + [3] arginine -urea

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Improved Synthesis of N-Alkyl-Aspartic Acids

Abstract: not available

Cited by 11 publications

References 1 publication

Amphoteric surfactants from mixed N‐alkylethylenediamine

Amphoteric surfactants from mixed N‐alkylethylenediamine

Enantioselective Synthesis of N‐Substituted Aspartic Acids Using an Engineered Variant of Methylaspartate Ammonia Lyase

Inhibition of urea cycle enzymes by aspartic acid analogues

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