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L-a-amino acid

In 1959 a new non-protein L-a-amino acid was isolated from the seeds of Acacia willardiana and later from other species of Acacia-, it proved to be l-/3-amino-/3-carboxyethyluracil (977) (59ZPC(316)164). The structure was confirmed by at least four syntheses in the next few years. The most important involves a Shaw synthesis (Section 2.13.3.1.2e) of the acetal (975) and hydrolysis to the aldyhyde (976) followed by a Strecker reaction (potassium cyanide, ammonia and ammonium chloride) to give DL-willardiine (977) after resolution, the L-isomer was identical with natural material (62JCS583). Although not unambiguous, a Principal Synthesis from the ureido acid (978) and ethyl formylacetate is the most direct route (64ZOB407). [Pg.146]

While the a-helix of L-a-peptides and the (M)-3i4 helix of the corresponding peptides have opposite polarity and helicity (see Section 2.2.3.1), the inserhon of two CH2 groups in the backbone of L-a-amino acids leave these two hehx parameters unchanged, both the a-helix and the 2.614-hehx of the resulting y" -peptides being right-handed and polarized from N to C terminus. In view of these similarities, the y-peptide hehcal fold might prove useful as a template to elaborate functional mimetics of bioachve a-polypeptides. [Pg.88]

Both D-amino acids and non-a-amino acids occur in nature, but only L-a-amino acids are present in proteins. [Pg.20]

Scheme 10.7 1,3-Dipolar cycloadditions of nitrones with 1,1-diethoxypropene catalysed by oxazaborolidines derived A-tosyl-L-a-amino acids. Scheme 10.7 1,3-Dipolar cycloadditions of nitrones with 1,1-diethoxypropene catalysed by oxazaborolidines derived A-tosyl-L-a-amino acids.
Fig. 9.6 Mirror image behaviour of enantiomeric molecules. The left-handed L-a-amino acid is converted to the right-handed D-a-amino acid by reflection... [Pg.248]

In a closely related study, Tung and Sun discussed the microwave-assisted liquid-phase synthesis of chiral quinoxalines [80], Various L-a-amino acid methyl ester hydrochlorides were coupled to MeOPEG-bound ortho-fluoronitrobenzene by the aforementioned ipso-fluoro displacement method. Reduction under microwave irradiation resulted in spontaneous synchronous intramolecular cyclization to the corresponding l,2,3,4-tetrahydroquinoxalin-2-ones (Scheme 7.71). Retention of the chiral moiety could not be monitored during the reaction, but after release of the desired products it was found that about 10% of the product had undergone racemization. [Pg.344]

Using this procedure, D- and L-a-amino acids have been enantiodifferentiated in the gas phase. ESI of hydroalcoholic solutions of the amino acid and CUCI2 into the source of an ion trap mass spectrometer reveals the presence of singly charged, covalently bound dimeric and trimeric ions. Table 10 reports the CID results of the diastereomeric complexes [A/ -Cu -(ref)2-H] and [As-Cu (ref)2-H]. ... [Pg.206]

New brush-type phases (donor-acceptor interactions) are appearing all the time. " Examples are stationary phases comprising quinine derivatives and trichloro-dicyanophenyl-L-a-amino acids as chiral selectors. Quinine carbamates, which are suitable for the separation of acidic molecules through an ionic interaction with the basic quinine group, are also commonly used but in general they are classified with the anion-exchange type of chiral selectors (see further) because of their interaction mechanism, even though r-donor, r-acceptor properties occur. (Some separations on Pirkle-type CSPs are shown in Table 2.)... [Pg.466]

Ribosomal synthesis of peptides proceeds through translation of messenger ribonucleic acid (mRNA) and utilizes the 20 primary L-a-amino acids. These amino acids are incorporated with the use of specific transfer ribonucleic acid (tRNA) codons. The 20 primary a-amino acids, with the exception of glycine that is achiral, are characterized by an L-configuration at the a-position (Figure 1). In general, most proteins are found to be composed of these 20 L-a-amino acids, as such they are referred to as protein amino acids. [Pg.5]

For the purpose of this chapter, all amino acids containing side chains that differ from the L-a-amino acids will be designated as either unusual or nonprotein amino acids. This is due to the observation that these unusual amino acids are generally not found to be the constituents of proteins. The scope of this chapter is limited to nonprotein L-a-amino acids. The definition of nonprotein amino acid is not absolute and, therefore, the... [Pg.5]

Figure 1 Stereochemical drawing and Fischer projection of an L-a-amino acid, where R is the side chain of the amino acid. Figure 1 Stereochemical drawing and Fischer projection of an L-a-amino acid, where R is the side chain of the amino acid.
Aryl side chain containing L-a-amino acids, such as phenylalanine (Phe), tyrosine (Tyr), and tryptophan (Trp), are derived through the shikimate pathway. The enzymatic transformation of phosphoenolpyr-uvate (PEP) and erythro-4-phosphate, through a series of reactions, yields shikimate (Scheme 2). Although shikimate is an important biosynthetic intermediate for a number of secondary metabolites, this chapter only describes the conversion of shikimate to amino acids containing aryl side chains. In the second part of the biosynthesis, shikimate is converted into chorismate by the addition of PEP to the hydroxyl group at the C5 position. Chorismate is then transformed into prephenate by the enzyme chorismate mutase (Scheme 3). [Pg.7]

In addition to this, it has been reported that nonprotein amino acids could be formed by structural modifications to protein amino acids (methylation, hydroxylation, and halogenation) through modified L-a-amino acid biosynthetic pathways and through novel biosynthetic routes. Some examples of the nonprotein amino acids derived through these biosynthetic pathways are given below (Figure 3). A detailed discussion of known biosyntheses for certain nonprotein amino acids will be discussed later in this chapter. [Pg.11]

During the biosynthesis of nonribosomal peptides, there are two ways to incorporate the nonprotein amino acids. They can be incorporated either as a single unit or as an L-a-amino acid, which then undergoes structural modifications, while attached to the carrier protein. In the case of coronamic acid, L-rr//o-isoleucine is loaded onto the carrier protein and a unique biosynthetic pathway produces a cyclopropyl group containing a nonprotein amino acid. Specific examples of the biosynthesis of nonprotein amino acids will be discussed in the following sections. [Pg.11]

The nonprotein amino acid, 1-aminocyclopropane-l-carboxylic acid, is an intermediate of ethylene biosynthesis in plants. This amino acid is synthesized from the L-a-amino acid methionine through the intermediate 5 -adenosyl-L-methionine (SAM) (Scheme 8). ... [Pg.12]

Nature utilizes the shikimate pathway for the biosynthesis of amino acids with aryl side chains. These nonprotein amino acids are often synthesized through intermediates found in the shikimate pathway. In many cases, L-a-amino acids are functionalized at different sites to yield nonprotein amino acids. These modifications include oxidation, hydroxylation, halogenation, methylation, and thiolation. In addition to these modifications, nature also utilizes modified biosynthetic pathways to produce compounds that are structurally more complex. When analyzing the structures of these nonprotein amino acids, one can generally identify the structural similarities to one of the L-a-amino acids with aromatic side chains. [Pg.19]

There is only a small selection of nonprotein amino acids that contain carbonyl groups in the form of ketone, aldehyde, and carboxylic acid moieties, as part of the side chain. The examples given in Table 6 are components of nonribosomal peptides isolated from bacteria or fungi and siderophores from bacteria. The biosynthesis of these amino acids is not clear however, some of the amino acids with carboxylic acid side chains may be traced back to the L-a-amino acids aspartic acid and glutamic acid. [Pg.32]

Substitution of the amino side-chain groups (R and R ) with any of the 20 endogenous L-a amino acids results in numerous potential chemical structures with varying degrees of biological activities. In addition, there are no limitations to the use of the D-enantiomers of the respective amino acids, thus adding to the number or multitude of permutations possible. [Pg.659]

Naturally air-fused DKPs are thermodynamically more stable, compared with their trawr-fused counterparts. This seems logical considering their biosynthetic origin, usually from two proteinogenic L-a-amino acids. Some other cis- and rntwr-functional DKPs are derived from nonproteinogenic D-a-amino acids. Naturally... [Pg.662]

Protein a polymer formed from a family of 20 common L-a-amino acids. [Pg.398]

The extension of the term isotactic to condensation polymers was made by Natta in his first article discussing poly-L-a-amino acids (22). In itself the term isotactic is redundant here as the configuration of the repeating unit is sufficient to identify the macromolecular stmcture. It is, however, useful to distinguish a system, racemic or not, in which each macromolecule is composed of only l or only D residues from a mixture of macromolecules made up of random or alternate sequences of L or d units. Similarly the term syndiotactic serves in the identification of oligopeptides or polypeptides composed of alternate sequences of D and L units, like those synthesized by Lorenzi and Tomasic (77). [Pg.12]


See other pages where L-a-amino acid is mentioned: [Pg.14]    [Pg.14]    [Pg.14]    [Pg.14]    [Pg.14]    [Pg.15]    [Pg.298]    [Pg.167]    [Pg.500]    [Pg.107]    [Pg.137]    [Pg.150]    [Pg.198]    [Pg.5]    [Pg.6]    [Pg.6]    [Pg.7]    [Pg.7]    [Pg.8]    [Pg.11]    [Pg.12]    [Pg.12]    [Pg.32]    [Pg.105]    [Pg.133]    [Pg.98]   
See also in sourсe #XX -- [ Pg.14 ]

See also in sourсe #XX -- [ Pg.33 ]

See also in sourсe #XX -- [ Pg.574 ]




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L amino acids

L,-a-Amino

L- -y-Amino-a-hydroxybutyric acid

Poly-L-a-amino acids

Protein A naturally occurring polymeric chain of L-amino acids linked together

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