Mycobacterium neoaurum ATCC amino amidase

A)-alcohol (7) by Sphingomonas paucimobilis SC 16113 (Fig. 6) (2) the enzymatic resolution of racemic (a-methyl)phenylalanine amide (8) and a-(4-methoxyphenyl)alanine amide (10) by amidase from Mycobacterium neoaurum ATCC 25795 to prepare the corresponding (S)-amino acids (9) and (11), and (3) the asymmetric hydrolysis of methyl-(4-methoxyphenyl)-propanedioic acid, diethyl ester (12), to the corresponding (X)-monoester (13) by pig liver esterase (Fig. 7). 

Enzymatic Resolution of Racemic a-Methyl Phenylalanine Amides. The chiral amino acids (22) and (23) (Fig. 6A) are intermediates for the synthesis of (33-receptor agonists (30,31). These are available via the enzymatic resolution of racemic a-methyl phenylalanine amide (24) and a-methyl-4-methoxy-phenylalanine amide (25), respectively, by an amidase from Mycobacterium neoaurum ATCC 25795 (32). Wet cells (10% wt/vol) completed the reaction of amide (24) in 75 min with a... 

III. AMINO AMIDASE FROM MYCOBACTERIUM NEOAURUM ATCC 25795... 

L-a-Amino acids have been prepared by the resolution of racemic a-amino acid amide by the L-specific aminopeptidase from Pseudomonas putida ATCC 12633 [7]. Enzyme from R putida ATCC 12633 cannot be used to resolve a-alkyl-substituted amino acid amides 103. Aminoamidase from Mycobacterium neoaurum ATCC 25795 has been used in the preparation of L-a-alkyl amino acid 104 (Fig. 34) and D-amide of a-alkyl-substituted amino acids by enzjmaatic resolution process using racemic a-alkyl amino acid amide as a substrate [169,179]. Amidase from Ochrobactrum anthropi catalyzed the resolution of a,a-disubsituted amino acids, iV-hydroxy amino acids, and a-hydroxy acid amides. The resolution process could lead to the production of chiral amino acids or amides in 50% yield. Recently, amino acid racemases have been used to get 100% yield of chiral amino acids [179]. 

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See also in sourсe #XX -- [ , , , ]

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