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Enzyme phenylalanine racemase

This enzyme [EC 5.1.1.11], also known as phenylalanine racemase (ATP-hydrolyzing), catalyzes the reaction of ATP with L-phenylalanine to produce o-phenylalanine, AMP, and pyrophosphate. In this unusual racemase reaction, a thiol group of an enzyme-bound pantotheine forms a thiolester from an initial aminoacyl-AMP intermediate then, as is typical of acyl thioesters, the a-proton becomes labile, thereby permitting reversible inversion of configuration to produce an equilibrated mixture of thiolester-bound enantiomers. Hydrolysis of the thiolester yields the product. [Pg.548]

J. Vater, and H. Kleinkauf, A further characterization of phenylalanine racemase, the light enzyme of gramicidin S-synthetase, Biochim. Biophys. Acta 429, 1062 (1976). [Pg.47]

Fluoro amino acids have been incorporated into peptides, in order to ease the transport or reduce the systemic toxicity. Thus, trifluoroalanine, a powerful inhibitor of alanine racemase, is an essential enzyme for the biosynthesis of the cell wall of bacteria. It has a low antibiotic activity because of its very poor transport. In order to facilitate this transport, the amino acid has been incorporated into a peptide. This delivery allows a reduction of the doses, and thus the toxicity of the treatment is lowered.3-FIuorophenylaIanine (3-F-Phe) is a substrate of phenylalanine hydroxylase, which transforms it into 3-F-Tyr. 3-F-Tyr has a high toxicity for animals, due to its ultimate metabolization into fluorocitrate, a powerful inhibitor of the Krebs cycle (cf. Chapter 7). 3-F-Phe has a low toxicicity toward fungus cells, but when delivered as a tripeptide 3-F-Phe becomes an efficient inhibitor of the growth of Candida albicans. This tripeptide goes into the cell by means of the active transport system of peptides, where the peptidases set free the 3-F-Phe. ... [Pg.171]

In addition, the amino acylase process can be also applied in the production of other proteinogenic and non-proteinogenic L-amino acids such as L-valine and l-phenylalanine. It is worth noting that racemases have recently been developed by several companies which allow (in combination with the L-aminoacylases) an extension of the existing process towards a dynamic kinetic resolution reaction [10]. It should be mentioned that the same concept can be also applied for the synthesis of D-amino acids when using a D-aminoacylase as an enzyme. [Pg.134]

The N-acetyl-D,L-amino acid precursors are conveniently accessible through either acetylation of D,L-amino acids with acetyl chloride or acetic anhydride in a Schotten-Baumann reaction or via amidocarbonylation I801. For the acylase reaction, Co2+ as metal effector is added to yield an increased operational stability of the enzyme. The unconverted acetyl-D-methionine is racemized by acetic anhydride in alkali, and the racemic acetyl-D,L-methionine is reused. The racemization can also be carried out in a molten bath or by an acetyl amino acid racemase. Product recovery of L-methionine is achieved by crystallization, because L-methionine is much less soluble than the acetyl substrate. The production is carried out in a continuously operated stirred tank reactor. A polyamide ultrafiltration membrane with a cutoff of 10 kDa retains the enzyme, thus decoupling the residence times of catalyst and reactants. L-methionine is produced with an ee > 99.5 % and a yield of 80% with a capacity of > 3001 a-1. At Degussa, several proteinogenic and non-proteinogenic amino acids are produced in the same way e.g. L-alanine, L-phenylalanine, a-amino butyric acid, L-valine, l-norvaline and L-homophenylalanine. [Pg.1441]


See other pages where Enzyme phenylalanine racemase is mentioned: [Pg.1140]    [Pg.120]    [Pg.1408]    [Pg.62]    [Pg.63]    [Pg.1296]    [Pg.168]    [Pg.88]    [Pg.99]    [Pg.49]    [Pg.574]   
See also in sourсe #XX -- [ Pg.1140 , Pg.1154 ]




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Phenylalanine enzyme

Racemase

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