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Aspartic acids

Aspartic acid is obtained in 90% yield from fumaric acid by using the aspartase enzyme  [Pg.32]

The -carboxylic acid group of aspartic acid has a pK of 3.86 and is ionized at pH 7.0 (the anionic form is called aspartate). The anionic carboxylate groups tend to occur on the surface of water-soluble proteins, where they interact with water. Such surface interactions stabilize protein folding. [Pg.23]

In the degradation of aspartic acid, the major pathway in the vertebrate organism appears to be its transamination to oxalacetic acid the latter is then oxidized by means of the TCA cycle. [Pg.83]

A number of alternate pathways exist for the metabolism of aspartic add. It can couple with dtruUine, forming arginosucdmc acid, which is subsequently cleaved to fumarate and ar nine IS). [Pg.83]

The carbamyl group of citrulline can also be transferred to L-aspartate, it is believed through carbamyl phosphate as an intermediate, to form carbamyl-L-asparate (16-18). This in turn is the precursor of dihydro-orotic acid and ultimately of the pyrimidines. [Pg.83]

An enz3une that oxidizes D-aspartic acid was discovered in rabbit kidney and liver by Still et dl. (19) and confirmed by Nakada and Weinhouse (iO). D-Aspartic acid oxidase is a soluble enzyme which can be obtained in hi concentration in the supernatant fluid of tissue homogenates. Althou no coenzyme requirement has been found for this enzyme, the fact that it forms H2O2 suggests that it contains a tightly bound flavin coenzyme. Unlike the D-amino acid oxidase of Krebs, D-aspartic acid oxidase is not inhibited by benzoate. [Pg.83]

Another pathway for the metabolism of aspartic acid found in microorganisms and plants, but not in the vertebrates, is through the action of the enzsrme aspartase (21-94a, b). This enzyme reversibly catalyzes the reaction  [Pg.83]

Asparagine, the amide of aspartic acid, was first isolated by Robi-quet and Vauquelin, in 1806, from the juice of Asparagus officinalis hence its name. Not only is asparagine found in asparagus, but also in the seedlings of lupines, peas, vetches, etc., from which it is best and most easily prepared. [Pg.51]

Aspartic acid.was first obtained by Plisson, in 1827, from asparagine by boiling it with lead hydroxide, and is usually prepared from this compound by hydrolysis with alkali or acid. [Pg.51]

Its composition, C H7N04, was established in 1833 by Boutron-Charlard and Pelouze, and confirmed by Liebig. In 1848 Piria showed that aspartic acid was converted into malic acid by the action of nitrous acid, and he regarded aspartic acid and asparagine as the two amides of malic acid [Pg.51]

COOH CONHj. CHj. CHOH. CONH  [Pg.51]

This idea of their constitution was proved to be erroneous by Kolbe in 1862, who showed that aspartic acid did not give off ammonia when boiled with dilute caustic alkali, and that asparagine only lost half of its nitrogen when thus treated. Aspartic acid was therefore not the amide of malic acid, but amino-succinic acid, and asparagine the amide of this compound. [Pg.51]

3 Analogues of A -Benzoyl-sj i-phenylisoserine, (5)-P-Homoserine and (iS)-Aspartic Acid [Pg.486]

An unusual metabolic reaction of glutamic acid is its decarboxylation to 7-aminobutyric acid. - This reaction is carried on very actively by brain tissue and leads to a considerable accumulation of the product in the brain. The decarboxylation of L-glutamate has been obtained with crude homogenates and extracts of acetone-dried powder of brain. The pH optimum of the reaction is at 6.8, and the enzyme is inhibited by cyanide, semicarbazide, and hydroxylamine. Aspartic acid is not attacked by the enzyme. [Pg.50]

The oxidation of L-aspartate (but not of the D-isomer) was accomplished by Nakada and Weinhouse with washed homogenates of rat liver, upon the addition of either AMP or ATP. The interpretation of the authors is that the oxidation of L-aspartate is not due to a specific oxidase, but that it is caused by the transamination of the amino acid to oxal-acetate, which is subsequently oxidized through the operation of the citric acid cycle. The occurrence of aspartic-glutamic transaminase was demonstrated by assay and by the accumulation of glutamic acid. [Pg.51]

Still and co-w orkers were unable to secure the oxidation of L-aspartic acid with rabbit liver cyclophorase preparations, although they discovered the occurrence of an enzyme in these preparations capable of oxidizing D-aspartate. [Pg.51]

This was verified by Nakada and Weinhouse, but they found, contrary to Still and associates, that the rabbit liver homogenates also oxidized L-asparate, and to about the same degree as the D-isomer. Moreover, in contrast to rat liver homogenate, which is soon inactivated upon incubation, the rabbit homogenate could continue oxidation of the aspartate at a linear rate for several hours. [Pg.51]

Triethyl a-phtholimidoethane-a,a,(t-tricarboxylate. Three hundred and twenty-seven grams (1.0 mole) of diethyl sodium phthalimidomalonate 1 and 735 g. (6.0 moles) of ethyl chloro-acetate (b.p. 144-145°) are placed in a 2-1. Claisen flask fitted with a reflux condenser and rubber stoppers. The mixture is heated under reflux in an oil bath at 150-160° for 2.25 hours. The excess ethyl chloroacetate is removed by distillation at 30 mm. until the heating bath temperature reaches 150° and no more distillate is obtained (Note 1). The brown residual mass is [Pg.7]

DL-Aspartic acid. A mixture of 383 g. of the above crude product, 1 1. of concentrated hydrochloric acid, 1 1. of glacial acetic acid, and 11. of water is boiled under reflux in a 5-1. round-bottomed flask for 2-3 hours. The reflux condenser is then replaced by a fractionating column, and the mixture is slowly distilled until the temperature at the head of the column has risen to 108°. This requires about 13 hours. The distillate amounts to 1.5 1. (Note 3). [Pg.8]

The crude DL-aspartic acid, amounting to 58-60 g., is recrys-tallizcd from 600 ml. of hot water and yields 54 g. of pure dl- [Pg.8]

Although this product cannot be purified by distillation, it contains almost the theoretical amount of nitrogen as shown by Kjeldahl analysis. [Pg.9]

During the first few hours the distillate contains ethyl acetate the distillate obtained during the first hour, amounting to 137 ml., distils below 99° and on saturation with sodium chloride yields 115 ml. of crude ethyl acetate. [Pg.9]


M.p. 234-235 C. Hydrolyses to aspartic acid. L-asparagine can be prepared from lupin seedlings, and DL-asparagine is synthesised from ammonia and maleic anhydride. L-asparagine is very widely distributed in plants, being found in all the Leguminosae and Gramineae, and in many other seeds, roots and buds. [Pg.43]

The naturally occurring substance is L-aspartic acid. One of the acidic-amino acids obtained by the hydrolysis of proteins. [Pg.43]

The data led to tire cycle shown in figure C2.7.8. Here, only tire active site on tire interior enzyme surface (section C2.6) is depicted, consisting of R groups including aspartic acid, glutamic acid and otliers, represented witli tire shortliand Asp, Glu etc tire subscripts represent tlie positions on tlie polypeptide chain. [Pg.2707]

Fig. 10.12 Sequence alignment of trypsin, chymotrypsin and thrombin (bovine). The active sites histidine, aspartic acid and serine are highlighted. Fig. 10.12 Sequence alignment of trypsin, chymotrypsin and thrombin (bovine). The active sites histidine, aspartic acid and serine are highlighted.
Glycine itself is almost neutral, and requires very little sodium hydroxide to give a pink colour with phenolphthalein some other amino-acids, e.g., glutamic acid, aspartic acid, etc., are definitely more acidic and consequently require more alkali for this purpose cf. footnote, p. 380). [Pg.463]

Aza-T-allylpalladium is formed from the Schiff base 193 and reacts with malonate to give a derivative of aspartic acid 194 after hydrolysis of the pro-duct[121]. [Pg.316]

Some ammo acids have side chains that bear acidic or basic groups As Table 27 3 indicates these ammo acids are characterized by three values The third pK reflects the nature of the side chain Acidic ammo acids (aspartic and glutamic acid) have acidic side chains basic ammo acids (lysine arginine and histidine) have basic side chains The isoelectric points of the ammo acids m Table 27 3 are midway between the pK values of the zwitterion and its conjugate acid Take two examples aspartic acid and lysine Aspartic acid has an acidic side chain and a pi of 2 77 Lysine has a basic side chain and a pi of 9 74... [Pg.1118]

Thus if a mixture containing alanine aspartic acid and lysine is subjected to electrophoresis m a buffer that matches the isoelectric point of alanine (pH 6 0) aspartic acid (pi = 2 8) migrates toward the positive electrode alanine remains at the origin and lysine (pi =9 7) migrates toward the negative elec trode (Figure 27 3b)... [Pg.1120]

IS placed at the center of a sheet of cellulose acetate The sheet is soaked with an aqueous solution buffered at a pH of 6 0 At this pH aspartic acid C ) exists as its — 1 ion alanine as its zwittenon and lysine as its +1 ion... [Pg.1120]

FIGURE 27 3 Application of electrophoresis to the separation of aspartic acid alanine and lysine according to their charge type at a pH corresponding to the isoelectric point (pi) of alanine... [Pg.1120]

Alanine (ala) Phenylalanine (phe) R 1 0 - HNCHC N General formula for an amino acid residue Aspartic Acid (asp)... [Pg.330]


See other pages where Aspartic acids is mentioned: [Pg.28]    [Pg.43]    [Pg.2697]    [Pg.182]    [Pg.538]    [Pg.380]    [Pg.439]    [Pg.439]    [Pg.183]    [Pg.1112]    [Pg.1114]    [Pg.1115]    [Pg.1118]    [Pg.1118]    [Pg.1119]    [Pg.537]    [Pg.857]    [Pg.1179]    [Pg.733]    [Pg.330]    [Pg.20]    [Pg.7]    [Pg.75]    [Pg.75]    [Pg.75]    [Pg.75]    [Pg.75]    [Pg.75]    [Pg.75]    [Pg.75]    [Pg.75]    [Pg.553]    [Pg.620]    [Pg.684]    [Pg.684]    [Pg.777]   
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A aspartic acid

A-methyl-D-aspartic acid

ASPARTIC ACID POLYMER

Acid, acetic aspartic

Amides Aspartic acid

Amides, of aspartic acid

Amino acid aspartate family

Amino acid aspartate transcarbamylase

Amino acid sequence of aspartate aminotransferase

Amino acid transmitters Aspartate, GABA, Glutamate

Amino acids L-aspartate

Amino acids aspartate

Amino acids aspartic and glutamic acid

Amino aspartic acid

Anti- Aspartic acid

Arginine, glycine and aspartic acid

Arginine-Glycine-Aspartic acid peptides

Arginine-glycine-aspartic acid

Arginine-glycine-aspartic acid improvement

Arginine-glycine-aspartic acid sequence

Arginine-glycine-aspartic acid-serine-lysine

Asparagine aspartic acid system

Aspartate fumaric acid

Aspartate/aspartic acid degradation

Aspartate/aspartic acid ionic properties

Aspartate/aspartic acid synthesis

Aspartic Acid (revised)

Aspartic Acid determination

Aspartic Acids and Arginines

Aspartic acid (Asp

Aspartic acid (Asp biosynthesis

Aspartic acid , ionisation

Aspartic acid -esters

Aspartic acid 1-Aspartyl peptides

Aspartic acid acylase

Aspartic acid anion

Aspartic acid benzyloxycarbonyl

Aspartic acid biochemical structure

Aspartic acid biosynthesis

Aspartic acid biotechnological production

Aspartic acid carbon catabolism

Aspartic acid characterisation

Aspartic acid cleavage

Aspartic acid configuration change

Aspartic acid constitution

Aspartic acid cytochrome

Aspartic acid decarboxylase

Aspartic acid deficiency

Aspartic acid degradation

Aspartic acid derivatives

Aspartic acid discovery

Aspartic acid dissociation constant

Aspartic acid dyad

Aspartic acid energy production

Aspartic acid from proteins

Aspartic acid hemoglobin

Aspartic acid intermediate

Aspartic acid ionization

Aspartic acid isoelectric point

Aspartic acid isolation

Aspartic acid kinase

Aspartic acid lactoglobulin

Aspartic acid lithium aluminum hydride modifiers

Aspartic acid manufacture

Aspartic acid metabolism

Aspartic acid metal complexes

Aspartic acid mixtures

Aspartic acid mucosa

Aspartic acid naturally occurring

Aspartic acid occurrence

Aspartic acid oxidase

Aspartic acid oxidation

Aspartic acid peptides

Aspartic acid peptides hydrolysis

Aspartic acid peptides naturally occurring

Aspartic acid physiological roles

Aspartic acid polypeptide

Aspartic acid prebiotic systems

Aspartic acid protease

Aspartic acid protein concentration

Aspartic acid purification

Aspartic acid reaction

Aspartic acid relative hydrophobicity

Aspartic acid residue location

Aspartic acid residues

Aspartic acid residues, reactivity

Aspartic acid resolution

Aspartic acid rotation

Aspartic acid sidechains

Aspartic acid solubility

Aspartic acid stereochemistry

Aspartic acid structural classification

Aspartic acid transition state analogs

Aspartic acid via reductive amination

Aspartic acid with transaminases

Aspartic acid, acetyl derivative

Aspartic acid, aspartimide formation

Aspartic acid, carbohydrate-based

Aspartic acid, carbon atom reactions

Aspartic acid, characteristics

Aspartic acid, chromatographic separation

Aspartic acid, deamination

Aspartic acid, decarboxylation

Aspartic acid, ionic forms

Aspartic acid, orthogonal protecting

Aspartic acid, production

Aspartic acid, racemization

Aspartic acid, specific rotation

Aspartic acid, structure

Aspartic acid, structure and properties

Aspartic acid, synthesis

Aspartic acid, titration

Aspartic acid-derived analog

Aspartic acid-proline sequence

Aspartic acid/asparagine

Aspartic acid/asparagine mixtures

Aspartic acid/aspartate

Aspartic acid/aspartate

Aspartic and Glutamic Acids

Aspartic maleic acid

BOC-L-Aspartic acid

Benzyloxycarbonyl-L-aspartic acid

Betulinic acid aspartic protease

C4H7NO4=Aspartic acid

Carbamyl aspartic acid

Carbamyl aspartic acid, biosynthesis

Carboxymethylated-aspartic acid

Casein aspartic acid racemization

Catalytic aspartic acids

Chiral precursors aspartic acid

Cysteine-aspartic acid protease-3 (caspase

D-Aspartic acid

Dimers arginine-aspartic acid

Dl-Aspartic acid

Ellagic acid aspartic protease

Endopeptidase aspartic acid

Fumarase aspartic acid

Glutamic and Aspartic Acid Residues

Glycosylamines coupling with aspartic acid

Glycyl-L-aspartic acid

Histidine copolymer with aspartic acid

I-aspartic acid

JV-methyl-D-aspartic acid

L Aspartic acid

L-aspartic acid peptides

Ligand binding aspartic acid

N- aspartic acid

N-Methyl-L-aspartic acid

N-methyl-D-aspartic acid

N-methyl-D-aspartic acid receptors

N-protected aspartic acids

Nickel complexes aspartic acid

Of L-aspartic acid

Of aspartic acid

Phthaloyl aspartic acid

Plasma aspartic acid

Poly-L-aspartic acid

Poly-a,p-aspartic acid

Production of aspartic and malic acids

Proteins aspartic acid

Purine aspartic acid

Pyrimidine Aspartic acid synthetase

Radiocarbon aspartic acid racemization

Sulfur mustard aspartic acid

Synthesis of L-Aspartic Acid

The Carboxyl Groups of Aspartic and Glutamic Acids

Threonine aspartic acid

Tripeptide arginine-glycine-aspartic acid

Urine aspartic acid

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