Valine manufacture

Enzymatic hydrolysis is also used for the preparation of L-amino acids. Racemic D- and L-amino acids and their acyl-derivatives obtained chemically can be resolved enzymatically to yield their natural L-forms. Aminoacylases such as that from Pispergillus OTj e specifically hydrolyze L-enantiomers of acyl-DL-amino acids. The resulting L-amino acid can be separated readily from the unchanged acyl-D form which is racemized and subjected to further hydrolysis. Several L-amino acids, eg, methionine [63-68-3], phenylalanine [63-91-2], tryptophan [73-22-3], and valine [72-18-4] have been manufactured by this process in Japan and production costs have been reduced by 40% through the appHcation of immobilized cell technology (75). Cyclohexane chloride, which is a by-product in nylon manufacture, is chemically converted to DL-amino-S-caprolactam [105-60-2] (23) which is resolved and/or racemized to (24)... 

There are 22 different AAs in the body of the bird, 10 of which are essential AA (EAA arginine, methionine, histidine, phenylalanine, isoleucine, leucine, lysine, threonine, tryptophan and valine), i.e. cannot be manufactured by the body and must be derived from the diet. Cystine and tyrosine are semi-essential in that they can be synthesized from methionine and phenyla-... 

Although all of the amino acids listed in Table SO-1 are present in the proteins of the human body, not all of them need to be in the food. Experiments have been carried out which show that nine of the amino acids are essential to man. 1 hese nine essential amino acids are histidine, lysine, tryptophan, phenylalanine, leucine, isoleucine, threonine, methionine, and valine. The human body seems to be able to manufacture the others, which are called the non-essential amino acids. Some organisms that we usually consider to be simpler than man have greater powers than the human organism, in that they are able to manufacture all of the amino acids from inorganic constituents. The red bread mold, Neurospora, has this power. 

The liver uses alanine, along with serine, to manufacture glucose. Phenylalanine, glycine and proline levels are not affected to any greater extent than that seen in other tissues. The concentrations of the branched chain amino acids isoleucine and valine in blood remain unchanged. 

Herbicidal sulfonylureas have a unique mode of action they interfere with a key enzyme required for plant cell growth - acetohydroxyacid synthase (AHAS, EC 2.2.1.6) [1, 2, 3] (see also Mark E. Thompson in this volume, Chapter 2.1 Biochemistry of the Target and Resistance ). AHAS is the enzyme responsible for the synthesis of the branched-chain amino acids valine, leucine and isoleucine. Inhibition of this enzyme disrupts the plant s ability to manufacture proteins, and this disruption subsequently leads to the cessation of all cell division and eventual death of the plant. 

Remarkably, nearly half of the amino acid components are L-a-amino-isobutyric acid residues (Aib), an amino acid not present in ribosome-manufactured proteins (p. 8). Peptides containing Aib-residues have been recognized to form a-helices particularly readily, an explanation of the pore forming properties of alamethicins and of similar natural and artificial polypeptides. In the natural analogs alanine or valine is found to be replaced by Aib closely related natural compounds are among others, suzukacillin, trichotoxin (mould products), and less similar, a component of bee venom, the 25-peptide mellitin. In the synthesis of peptides containing a-amino-isobutyric acid certain difficulties are encountered due to the poor steric accessibility of the amino—as well as of the carboxyl group. 

Degussa/Rexim, partly in collaboration with Chinese manufacturers, produce (L)-threonine, (L)-valine and (L)-isoleucine by fermentation. [62] With genetically modified strains from Echerichia coli and Serratia marcescens, they are able to achieve end concentrations of 100 grams per litre. 

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