And glutamate

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... 

A persistent idea is that there is a very small number of flavor quaUties or characteristics, called primaries, each detected by a different kind of receptor site in the sensory organ. It is thought that each of these primary sites can be excited independently but that some chemicals can react with more than one site producing the perception of several flavor quaUties simultaneously (12). Sweet, sour, salty, bitter, and umami quaUties are generally accepted as five of the primaries for taste sucrose, hydrochloric acid, sodium chloride, quinine, and glutamate, respectively, are compounds that have these primary tastes. Sucrose is only sweet, quinine is only bitter, etc saccharin, however, is slightly bitter as well as sweet and its Stevens law exponent is 0.8, between that for purely sweet (1.5) and purely bitter (0.6) compounds (34). There is evidence that all compounds with the same primary taste characteristic have the same psychophysical exponent even though they may have different threshold values (24). The flavor of a complex food can be described as a combination of a smaller number of flavor primaries, each with an associated intensity. A flavor may be described as a vector in which the primaries make up the coordinates of the flavor space. 

Cyclic anhydddes aie formed readily from Al-protected aspartic and glutamic acids. 

The first are competitors of PABA (p-aminobenzoic acid) and thus intermpt host de novo formation of the tetrahydrofoUc acid required for nucleic acid synthesis. Examples of dmgs that fall into this group are the sulfones and sulfonamides. The most weU-known of the sulfones is dapsone (70, 4,4 -diaminodiphenyl sulfone, DDS), whose toxicity has discouraged its use. Production of foHc acid, which consists of PABA, a pteridine unit, and glutamate, is disturbed by the substitution of a sulfonamide (stmcturally similar to PABA). The antimalarial sulfonamides include sulfadoxine (71, Fanasd [2447-57-6]) sulfadiazine (25), and sulfalene (72, sulfamethoxypyrazine [152-47-6] Kelfizina). Compounds of this group are rapidly absorbed but are cleared slowly. 

Oxazolidines are prepared to allow selective protection of the ct- or aj-C02H groups in aspartic and glutamic acids. 

L-Lysine monohydrochloride [657-27-2] M 182.7, [a] as above. Likely impurities are arginine, D-lysine, 2,6-diaminoheptanedioic acid and glutamic acid. Crystd from water at pH 4-6 by adding 4 volumes of EtOH. Above 60% relative humidity it forms a dihydrate. 

The side chains of the 20 different amino acids listed in Panel 1.1 (pp. 6-7) have very different chemical properties and are utilized for a wide variety of biological functions. However, their chemical versatility is not unlimited, and for some functions metal atoms are more suitable and more efficient. Electron-transfer reactions are an important example. Fortunately the side chains of histidine, cysteine, aspartic acid, and glutamic acid are excellent metal ligands, and a fairly large number of proteins have recruited metal atoms as intrinsic parts of their structures among the frequently used metals are iron, zinc, magnesium, and calcium. Several metallo proteins are discussed in detail in later chapters and it suffices here to mention briefly a few examples of iron and zinc proteins. 

Figure 1.9 Examples of functionally important intrinsic metal atoms in proteins, (a) The di-iron center of the enzyme ribonucleotide reductase. Two iron atoms form a redox center that produces a free radical in a nearby tyrosine side chain. The iron atoms are bridged by a glutamic acid residue and a negatively charged oxygen atom called a p-oxo bridge. The coordination of the iron atoms is completed by histidine, aspartic acid, and glutamic acid side chains as well as water molecules, (b) The catalytically active zinc atom in the enzyme alcohol dehydrogenase. The zinc atom is coordinated to the protein by one histidine and two cysteine side chains. During catalysis zinc binds an alcohol molecule in a suitable position for hydride transfer to the coenzyme moiety, a nicotinamide, [(a) Adapted from P. Nordlund et al., Nature 345 593-598, 1990.)...

Many proteins contain intrinsic metal atoms that are functionally important. The most frequently used metals are iron, zinc, magnesium, and calcium. These metal atoms are mainly bound to the protein through the side chains of cysteine, histidine, aspartic acid, and glutamic acid residues. 

The 20 common amino acids can be further classified as neutral, acidic, or basic, depending on the structure of their side chains. Fifteen of the twenty have neutral side chains, two (aspartic acid and glutamic acid) have an extra carboxylic acid function in their side chains, and three (lysine, arginine, and histidine) have basic amino groups in their side chains. Note that both cysteine (a thiol) and tyrosine (a phenol), although usually classified as neutral amino acids, nevertheless have weakly acidic side chains that can be deprotonated in strongly basic solution. 

The importance of Heinrich Ritthausen s fundamental studies, 1862 to 1899, on analytical procedures for the determination of amino acids in proteins has been emphasized in the biographical sketches which have been presented by Osborne (210), Vickery (289), and Chibnall (47). It is of particular interest to note here the prediction made by Ritt-hausen about 1870 that the amino acid composition would prove to be the most adequate basis for the characterization of proteins. Ritthausen and Kreusler (230) were the first, in 1871, to determine amino acids derived from proteins, and some of the values which they found for aspartic and glutamic acids are given in Table III (cited by Chibnall, 47, and Vickery, 286). 

Based on the use of 2 (R1 = H), metalated with two equivalents of potassium tert-butoxide in tetrahydrofuran, routes to (S)-phosphinotricin (79% ee) and glutamic acid (69% ee) were developed211. 

PRODUCTION OF AMINO ACIDS (LYSINE AND GLUTAMIC ACID) AND INSULIN... 

Substrate specificity is determined by high affinity for the cognate neurotransmitter substrate. However, low affinity uptake does also have a part in the clearance of transmitters from the interstitial space (e.g., in uptake mediated by the extraneuronal monoamine transporter, EMT) and in the intestinal absoiption of glycine and glutamate. It is obvious that there is an evolutionary relation of neurotransmitter transporters and amino acid and cation transporters in epithelia. 

The exocytotic release of neurotransmitters from synaptic vesicles underlies most information processing by the brain. Since classical neurotransmitters including monoamines, acetylcholine, GABA, and glutamate are synthesized in the cytoplasm, a mechanism is required for their accumulation in synaptic vesicles. Vesicular transporters are multitransmembrane domain proteins that mediate this process by coupling the movement of neurotransmitters to the proton electrochemical gradient across the vesicle membrane. 

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