Glutamic acid Glu Glutamate

The synthesis of N-labeled glutamic acid (glutamate [Glu, E]) has been reported to be effectively accomplished by mixing 2-ketoglutaric acid (a-ketoglutaric acid) in aqueous solution with N-enriched ammonium chloride and dilute sodium hydroxide. Then, as shown in Scheme 12.31, when that mixture is added dropwise over a period of about 5h to a suspension of reduced platinum oxide in water,... 

Ferritin is a globular iron-storage protein that stores iron as FeJ+. To leave the ferritin, Fe3+ must first be reduced to Fe2+. Ferritin has two types of channels through which the Fe"+ could leave a three-fold channel and a four-fold channel. The three-fold channel is lined with the amino acids aspartate (Asp) and glutamate (Glu) and the four-fold channel is lined with the amino acid leucine (Leu). Through which channel is the Fe + more likely to leave the ferritin protein Explain your answer. 

Figure 28 A dendrimer-based approach for the design of globular protein mimic using glutamic (Glu) and aspartic (Asp) acids as the building blocks and adamantyl as the core [151].

L-Aspartic acid or aspartate (ASP or D) L-Glutamic acid or glutamate (GLU or E)... 

The proteinogenic amino acid glutamate (Glu) and the biogenic amine 4-aminobuty-rate derived from it are among the most important neurotransmitters in the brain (see p. 352). They are both synthesized in the brain itself In addition to the neurons, which use Glu or GABA as transmitters, neuroglia are also involved in the metabolism of these substances. 

Glutamate (Glu) is the most abundant amino acid in the central nervous system (CNS). It serves many functions as an intermediate in neuronal metabolism, e.g., as a precursor for GABA. About 30% of the total glutamate in the brain functions as the major excitatory neurotransmitter. 

The direction of enantio-differentiation (the predominant enantiomer R or S, to be produced) is decided by two factors. One factor is the configuration of the chiral structure, that is, if the catalyst modified with (S)-glutamic acid [(S)-Glu-MRNi] produces (R)-MHB from MAA, then (R)-Glu-MRNi produces (S)-MHB (2). The other factor is the nature of X. That is, when the amino acid or hydroxy acid with the same configuration is used as the modifying reagent, the configurations of the predominant products are enantiomers of each other in most cases. For example, (S)-aspartic acid-MRNi produces (R)-MHB and (S)-malic acid-MRNi produces (S)-MHB (19). 

FIGURE 8—16. Gamma-aminobutyric acid (GABA) is produced by synthesis from the precursor amino acid glutamate by the enzyme glutamic acid decarboxylase (Glu-AD). 

Recently, the difference in structure and chemical reactivity between 2-D racemic and enantiomorphous crystallites has been used to generate enan-tiopure homochiral oligopeptides from non-racemic mixtures of amphiphilic a-amino acid NCAs. The racemic N"-carboxyanhydridc of y-slcaryl-glutamic acid (Cis-Glu-NCA) self-assembles on water to form racemic 2-D crystallites (Fig. 16a,b), as proved by GIXD. 

The C helix forms the back wall of the ATP-binding site [9]. It contains a conserved glutamic acid residue (Glu-52), which is of key importance in the phosphotransfer process, forming an ion pair with Lys-33 (Figure 7.3). Lys-33, which is buried deep in the ATP-binding cleft, makes a crucial contact with the a,P-phosphate oxygens, positioning them so as to facilitate the y-phosphoryl transfer [4 (i)]. 

The two conserved, buried glutamates Glu-14, Glu-152 have clear functional roles, each orienting four carbonyls of successive amino acids in the vestibules. The conserved pair of group III Gly-64 and Gly-199 are symmetrically located at the extremities of the central selective filter and serve to structure the downturn of the extended chains from 65 to 68 and 200 to 203 that form the critical line of four carbonyls each that in turn provide the pitons for successive hydrogen bond donors on their way through the channel (Fig. 3). 

---