Arginine-glycine-asparagine acid

The non-essential amino acids are alanine, arginine, aspartate, asparagine, cysteine, glutamate, glutamine, glycine, proline, serine and tyrosine. A summary of the reactions involved in their synthesis is given in Figure 8.3 and full details of these pathways are provided in Appendix 8.2. 

Ala Alanine Arg Arginine Asn Asparagine Asp Aspartic Acid Cys Cysteine Gin Glutamine Glu Glutamic Acid Gly Glycine His Histidine lie Isoleucine... 

Lysine, arginine, proline, tyrosine, tryptophan, methionine, valine, phenylalanine, leucine, glutamic acid, glycine, asparagines, threonine and alanine are found in chilli. Asparagine, glutamine, glutamic acid and tryptophan account for 95% of the free amino acids. A small amount of aspartic acid... 

Fig. 20. Primary structure of hen-egg lysozyme. ALA alanine, ARG arginine, ASN asparagine, ASP aspartic acid, CYS cysteine, GLN glutamine, GLU glutamic acid, GLY glycine, HIS histidine, ILE isoleucine, LEU leucine, LYS lysine, MET methionine, PHE phenylalanine, PRO proline, SER serine, THR threonine, TRP tryptophan, TYR tyrosine, VAL valine. (Redrawn from Canfield and Lu, 1965).

It follows that the array of codons represents the instructions for producing 20 amino acids, the so-called common amino acids. These amino acids are named and symbolized as alanine (Ala), arginine (Arg), asparagine (Asn), aspartate (Asp), cysteine (Cys), glutamine (Gin), glutamate (Glu), glycine (Gly), histamine (His), isoleucine (lie), leucine (Leu), lysine (Lys), methionine (Met), phenylalanine (Phe), proline (Pro), serine (Ser), threonine (Thr), tryptophan (Trp), tyrosine (Tyr), and valine (Val). 

Fig. 1. The R, values in paper chromatography for the protein amino acids including cystine and for a-aminobutyric acid. I. Solvent butanol-acetic acid-water (12 3 5), 2. solvent phenol-water-conc. NH, aq (120 30 1). I, Alanine 2, a-aminobutyric acid 3, arginine 4, asparagine 5. aspartic acid 6, cysteine 7, cystine 8, glutamic acid 9, glutamine 10, glycine II, histidine 12, isoleucine 13, leucine 14, lysine 15, methionine 16, phenylalanine 17, proline 18, serine 19, threonine 20, tryptophan 21, tyrosine 22, valine. I, Area for acid amino acids II, area for neutral amino acids III, area for basic amino acids and amines.

L-Alanine L-Arginine L-Asparagine L-Glutamic acid L-Glutamine Glycine L-Histidine L-lsoleucine L-Leucine L-Methionine... 

On the basis of whole-animal nutritional studies, 14 amino acids are conventionally considered as essential for cultured cells arginine, cysteine, cystine, glutamine, histidine, isoleucine, leucine, lysine, methionine, phenylalanine, threonine, tryptophan, tyrosine, and valine. Conversely, the naturally occurring nonessential amino acids include alanine, serine, asparagine, proline, glycine, aspartic acid, and glutamic acid. Nutritional requirements for amino acids vary, both quantitatively and qualitatively, with cell type, culture condition, and genetic modification. 

Amino acids (L-alanine L-asparagine L-arginine L-aspartic acid L-cysteine L-glutamic acid L-glutamine L-glycine L-histidine L-isoleucine L-lysine ... 

Figure 4.4 Release of amino acids from cortical slices exposed to 50 mM K+. Measurements by HPEC and fluorescence detection after reaction of amino acids with o-phthalaldehyde 1, aspartate 2, glutamate 3, asparagine 4, serine 5, glutamine 6, histidine 7, homoserine (internal standard) 8, glycine 9, threonine 10, arginine 11, taurine 12, alanine 13, GABA 14, tyrosine. Glutamate concentration is almost 1 pmol/gl which represents a release rate of 30 pmol/min/mg tissue...

Included amino acids were alanine, arginine, aspartic acid, asparagine, glutamine, glutamic acid, glycine, histidine, isoleucine, leucine, lysine, methionine, phenylalanine, proline, serine, threanine, tryptophan, tyrosine, and valine. 

The interaction with both synthetic and naturally occurring amino acids has been studied extensively glycine (138, 173, 219-221), a-(173, 219) and /3-alanine (138, 220), sarcosine (219), serine (222), aspartic acid (138, 173, 222-226), asparagine (222), threonine (222), proline (219), hydroxyproline (219), glutamic acid (138, 222-225), glutamine (222), valine (219, 227), norvaline (219), methionine (222, 226), histidine (228, 229), isoleucine (219), leucine (219, 230), norleu-cine (219), lysine (222), arginine (222), histidine methyl ester (228), phenylalanine (138, 222), tyrosine (222), 2-amino-3-(3,4-dihydroxy-phenyl jpropanoic acid (DOPA) (222), tryptophan (222), aminoiso-butyric acid (219), 2-aminobutyric acid (219,231), citrulline (222), and ornithine (222). 

Figure 2.9. Amino acid sequences of human defensins. The conserved positions of six cysteine residues are shown in hatched boxes. Abbreviations A, alanine C, cysteine D, aspartic acid E, glutamic acid F, phenylalanine G, glycine H, histidine I, isoleucine K, lysine L, leucine M, methionine N, asparagine P, proline Q, glutamic acid R, arginine S, serine T, threonine V, valine W, tryptophan Y, tyrosine.

In addition to the amino acids described above, several other amino acid residues are also reactive toward compounds containing heavy atoms. These are the side chains of arginine, asparagine, glutamine, lysine, tryptophan, and tyrosine. Those that are not reactive are alanine, glycine, isoleucine. 

Figure 9-3. Fates of the carbon skeletons upon metabolism of the amino acids. Points of entry at various steps of the tricarboxylic acid (TCA) cycle, glycolysis and gluconeogenesis are shown for the carbons skeletons of the amino acids. Note the multiple fates of the glucogenic amino acids glycine (Gly), serine (Ser), and threonine (Thr) as well as the combined glucogenic and ketogenic amino acids phenylalanine (Phe), tryptophan (Trp), and tyrosine (Tyr). Ala, alanine Cys, cysteine lie, isoleucine Leu, leucine Lys, lysine Asn, asparagine Asp, aspartate Arg, arginine His, histidine Glu, glutamate Gin, glutamine Pro, proline Val, valine Met, methionine.

Based on the properties of the side chains, the 20 amino acids can be put into six general classes. The first class contains amino acids whose side chains are aliphatic, and is usually considered to include glycine, alanine, valine, leucine, and isoleucine. The second class is composed of the amino acids with polar, nonionic side chains, and includes serine, threonine, cysteine, and methionine. The cyclic amino acid proline (actually, an imino acid) constitutes a third class by itself. The fourth class contains amino acids with aromatic side chains tyrosine, phenylalanine, and tryptophan. The fifth class has basic groups on the side chains and is made up of the three amino acids lysine, arginine, and histidine. The sixth class is composed of the acidic amino acids and their amides aspartate and asparagine, and glutamate and glutamine. 

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