Discovery of amino acids

The history of the discovery of amino acids is closely related to advances ia analytical methods. Initially, quantitative and qualitative analysis depended exclusively upon crystallization from proteia hydrolysates. The quantitative precipitation of several basic amino acids including phosphotungstates, the separation of amino acid esters by vacuum distillation, and precipitation by sulfonic acid derivatives were developed successively duriag the last century. 

Since the discovery of amino acids in animal and plant proteins in the nineteenth century, most amino acids have been produced by extraction from proteia hydroly2ates. However, there are many problems in the efficient isolation of the desired amino acid in the pure form. 

Table 1. Taste, Threshold Value and Discovery of Amino Acids...

Although the discovery of amino acid formation was of tremendous significance in establishing that the raw materials of proteins were easy to obtain in a primitive Earth environment, there remained a larger question as to the nature of the origin of genetic materials—in particular the origin of DNA and RNA molecules. 

In particular, it was the discovery of amino acids and the percentages of the differing types of amino acids... 

T. Pederson, 50 years ago protein synthesis met molecular biology the discoveries of amino-acid activation and transfer RNA, FASEB J. 2005, 19, 1583. 

From H.B. Vickery, The history of the discovery of amino acids II. Advan. Protein Chem. 26 82-173 (1972)... 

Since the discovery of amino acid uptake in mitochondria, several investigators have attempted to demonstrate the presence of nucleic acids in mitochondria. 

Threonine is the third limiting amino acid after lysine and methionine in the animal feeds and was discovered by WC.Rose. Since the discovery of amino acid producers by Kinoshita, the major share of commercially produced threonine employs fermentative production. 

Asano, Y. and Yamaguchi, S., "Discovery of amino acid amides as new substrates for a-amino-e-caprolactam racemase horn Achromobacter oboe.". Mol. Catal. B Enzym., 36,22-29 (2005). 

The discovery of ribozymes (Section 28.11) in the late 1970s and early 1980s by Sidney Altman of Yale University and Thomas Cech of the University of Colorado placed the RNA World idea on a more solid footing. Altman and Cech independently discovered that RNA can catalyze the formation and cleavage of phosphodiester bonds—exactly the kinds of bonds that unite individual ribonucleotides in RNA. That, plus the recent discovery that ribosomal RNA catalyzes the addition of amino acids to the growing peptide chain in protein biosynthesis, takes care of the most serious deficiencies in the RNA World model by providing precedents for the catalysis of biological processes by RNA. 

Figure 1. An unrooted phylogenetic tree of the myosins based on the amino acid sequence comparison of their head domains demonstrating the division of the myosin superfamily into nine classes. The lengths of the branches are proportional to the percent of amino acid sequence divergence and a calibration bar for 5% sequence divergence is shovk n. The different classes of myosins have been numbered using Roman numerals in rough order of their discovery and hypothetical models of the different myosin structures are shown. Question marks indicate either hypothetical or unknown structural features, and only a fraction of the known myosins are shown. (Taken, in modified form, from Cheney et al., 1993).

The field of synthetic enzyme models encompasses attempts to prepare enzymelike functional macromolecules by chemical synthesis [30]. One particularly relevant approach to such enzyme mimics concerns dendrimers, which are treelike synthetic macromolecules with a globular shape similar to a folded protein, and useful in a range of applications including catalysis [31]. Peptide dendrimers, which, like proteins, are composed of amino acids, are particularly well suited as mimics for proteins and enzymes [32]. These dendrimers can be prepared using combinatorial chemistry methods on solid support [33], similar to those used in the context of catalyst and ligand discovery programs in chemistry [34]. Peptide dendrimers used multivalency effects at the dendrimer surface to trigger cooperativity between amino acids, as has been observed in various esterase enzyme models [35]. 

These are exciting times for peptide based materials. The number of investigators in this field and consequently the number of publications in this area have increased tremendously in recent years. Not since the middle of the past century has there been so much activity focused on the physical properties of peptidic materials. Then, efforts were focused on determination of the fundamental elements that make up protein structures, leading to the discoveries of the a—helix and the (3-sheet. Many years of study followed where the propensities of individual and combinations of amino acids to adopt and stabilize these structures were investigated. Now, this knowledge is being applied to the preparation, assembly, and use of peptide based materials with designed sequences. This volume summarizes recent developments in all these areas. 

Hydroxynitrile lyases (HNLs or oxynitrilases) catalyze C—C bond-forming reactions between an aldehyde or ketone and cyanide to form enantiopure cyanohydrins (Figure 1.15), which are versatile building blocks for the chiral synthesis of amino acids, hydroxy ketones, hydroxy acids, amines and so on [68], Screening of natural sources has led to the discovery of both... 

In the context of the discovery of amines and oxygen-containing organic compounds, the question arises as to whether the presence of atomic carbon in olivine or MgO crystals could have led to the formation of amino acids. Knobel et al. (1984) reported the detection of amino acids in liquid extracts of the reaction mixtures at the 1983 ISSOL conference yields were, however, extremely low, the total yield being 1.5-3.0 x 10-7 g per gram of MgO. These results were the subject of considerable attention in the media. 

Perhaps the one major drawback with DIPAMP is the long synthetic sequence required for its preparation, though shorter and cheaper methods are now available [12]. The ligand continues to be a player for the synthesis of amino acid derivatives at scale, including L-Dopa, as mentioned above [12, 25, 27-29]. Its continued use is a testament to the power of the initial discoveries, as well as showing that a chemical catalyst can achieve selectivities only previously seen with enzymes. 

Isolation of individual amino acids started about 1820 by 1904 all of the naturally occurring amino acids in proteins had been isolated except methionine (Mueller, 1922) and threonine (Rose, 1937). One of the earliest methods for the separation of amino acids was through the differential volatility of their methyl or ethyl esters (Emil Fischer, 1901). This approach led to the discovery of valine, proline, and hydroxyproline. [In the 1970s Fischer s method was modified for microanalysis of proteins, separating the amino acid esters by gas phase chromatography. Separation is now usually performed by hplc (high pressure liquid chromatography).]... 

The History of the Discovery of the Amino Acids. II. A. Review of Amino Acids Described Since 1931 as Components of Native Proteins Hubert Bradtord Vickery... 

The discovery that metal ions such as Cu catalyzed the hydrolysis of amino acid esters was first reported nearly 40 years ago. Table 6.3 shows that in the absence of direct interaction of the ester grouping with the metal ion, the primary cause of any increased rates experienced... 

---