L-Threonine

Amino acids are the main components of proteins. Approximately twenty amino acids are common constituents of proteins (1) and are called protein amino acids, or primary protein amino acids because they are found in proteins as they emerge from the ribosome in the translation process of protein synthesis (2), or natural amino acids. In 1820 the simplest amino acid, glycine, was isolated from gelatin (3) the most recendy isolated, of nutritional importance, is L-threonine which was found (4) in 1935 to be a growth factor of rats. The history of the discoveries of the amino acids has been reviewed... 

The nutritional value of a proteia can be improved by the addition of amino acids of low abundance ia that proteia. Thus the fortification of plant proteias such as wheat, com, and soybean with L-lysiae, DL-methionine, or other essential amino acids (L-tryptophan and L-threonine) is expected to alleviate some food problems (11). Such fortification has been widespread ia the feedstuff of domestic animals. 

Many kinds of amino acids (eg, L-lysine, L-omithine, t-phenylalanine, L-threonine, L-tyrosine, L-valine) are accumulated by auxotrophic mutant strains (which are altered to require some growth factors such as vitamins and amino acids) (Table 6, Primary mutation) (22). In these mutants, the formation of regulatory effector(s) on the amino acid biosynthesis is genetically blocked and the concentration of the effector(s) is kept low enough to release the regulation and iaduce the overproduction of the corresponding amino acid and its accumulation outside the cells (22). 

Mutation. For industrial appHcations, mutations are induced by x-rays, uv irradiation or chemicals (iiitrosoguanidine, EMS, MMS, etc). Mutant selections based on amino acid or nucleotide base analogue resistance or treatment with Nystatin or 2-deoxyglucose to select auxotrophs or temperature-sensitive mutations are easily carried out. Examples of useful mutants are strains of Candida membranefaciens, which produce L-threonine Hansenu/a anomala, which produces tryptophan or strains of Candida lipolytica that produce citric acid. An auxotrophic mutant of S. cerevisiae that requires leucine for growth has been produced for use in wine fermentations (see also Wine). This yeast produces only minimal quantities of isoamyl alcohol, a fusel oil fraction derived from leucine by the Ehrlich reaction (10,11). A mutant strain of bakers yeast with cold-sensitive metaboHsm shows increased stabiUty and has been marketed in Japan for use in doughs stored in the refrigerator (12). 

A second, conceptually distinct chiral synthesis of monobactams was developed from P-hydroxy amino acids. As shown in Figure 2, cycli2ation of the acylsulfamate of an amino-protected 0-mesylserine derivative (14, R = H) leads directiy to the monobactam (15). This methodology was also appHed to the synthesis of 4a- (15, R = CH ) and 4P-methyl monobactams from L-threonine and aHothreonine, respectively (17). The... 

Almost all actinomycins have the same chromophore, a planar phenoxa2inone dicarboxyUc acid called actinocin. In dactinomycin, the stmcture of which is shown in Figure 12, the two pendent pentapeptide lactones are identical, but in other actinomycins these lactones may be different. In other actinomycins the first amino acid, amide linked with actinocin, is usually L-threonine, as in dactinomycin the second position is sometimes D-aHo-isoleucine instead of D-valine the third position may be sarcosine or oxoproline the fourth position is sarcosine and the fifth position is sometimes /V-methyl isoleucine instead of /V-methylvaline. The lactone ring is always present. 

L-threonine deaminase [9024-34 ] 4.2.1.16 L-threonine — 2-ketobutyric acid + NH3 antineoplastic... 

Phospho-L-threonine (L-threonine-O-phosphate) [1114-81-4] M 199.1, m 194 (dec), [a]p -7.37 (c 2.8, H2O) (pK as above). Dissolve in the minimum volume of H2O, add charcoal, stir for a few min, filter and apply onto a Dowex 50W (H" " form) then elute with 2N HCI. Evaporate the eluates under reduced pressure whereby the desired fraction produced crystals of the phosphate which can be recrystd from H2O-MeOH mixtures and the crystals are then dried in vacuo over P2O5 at 80 . [de Verdier Acta Chem Scand 7 196 7955.]... 

Amino-4,6-dimethyl-3-oxo-3//-phenoxazine-l,9-dicarboxylic acid also named actinocin is the chromophor of the red antineoplastic chromopeptide aetinomyein D (formula A). Two cyclopenta-peptide lactone rings (amino acids L-threonine, D-valine, L-proline, sarcosine, and 7V-methyl-L-valine) are attached to the carboxy carbons of actinocin by two amide bonds involving the amino groups of threonine. 

It is a peptide containing 27 amino acid residues containing the amino acids L-histidine (His) L-aspartic acid (Asp) L-serine (Ser) glycine (Gly) L-threonine (Thr) L-phenyl-alanine (Phe) L-glutamic acid (Glu) L-glutamine [Glu(NHj)] L-leucine (Leu) L-arginine (Arg) L-alanine (Ala) and L-valinamide (Va -NHj). 

Auxotrophic mutants are used in the production of end products of branched pathways, ie pathways leading to more than one amino add at the same time. This is the case for L-lysine, L-methicmine, L-threonine and L-isoleudne in Brevibacterium flavum and Corynebacterium glutamicum. 

L-threonine adsorbtion and elution with aquous ammonia. 

This type of yvn-seleclivc aldol addition has been applied in the synthesis of the unusual L-threonine based amino acid, (2,S, 3/ ,6F)-3-hydroxy-4-methyl-2-methylamino-6-octenoic acid, of cyclosporine104, of the cyclic hexapeptide echinocandin105, and of the antibiotic ionomycin97. 

The L-threonine (EC 4.1.2.5), D-threonine (EC 4.1.2.-) or L-allothreonine aldolases (EC 4.1.2.6 synonymous to S1IMT) can be used for resolution of racemic (allo)threonine mixtures by highly selective cleavage of the unwanted isomers42, but can also efficiently direct the anabolic pathways. The substrate spectrum includes propanal, butanal and dodecanal43. 

Similar experiments suggested that 4-hydroxy-L-threonine (43) was an intermediate in synthesis of the three-carbon unit, C-6, C-5, C-5 (after decarboxylation). This was rigorously proved by a chemical synthesis of 4-hydroxy-L-(2,3-13C2)threonine. Incubation of E. coli mutant WG2 with this substrate produced a sample of pyridoxol that was examined by l3C NMR. The presence of doublets in the signals originating from C-5 and C-6 of pyridoxol exclusively, showed that the C-2-C-3 bond of the substrate had been incorporated intact into the predicted site (Scheme 18).42... 

The metabolism of P-hydroxy-a-amino adds involves pyridoxal phosphate-dependent enzymes, dassified as serine hydroxymethyltransferase (SHMT) (EC 2.1.2.1) or threonine aldolases (ThrA L-threonine selective = EC 4.1.2.5, L-aHo-threonine selective = EC 4.1.2.6). Both enzymes catalyze reversible aldol-type deavage reactions yielding glycine (120) and an aldehyde (Eigure 10.45) [192]. 

Ar-(rerr-butyloxycarbonyl)piperidin-4-yl]butyl bromide (C,4H26BrN02 142355-81-5) see Tirofiban hydrochloride -Terr-butyloxycarbonyl-L-threonine... 

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