Mycobacterium ATCC

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). 

These mutants are protected by several patent publications, e.g., Mycobacterium species CBS174 obtained from Mycobacterium species NRRL, Mycobacterium vaccae ZIMET 11052175 obtai ned from M. vaccae NRRL-B-3805, Mycobacterium roseum sp. nov. 1108/1 176, and Mycobacterium fortuitum NRRL-B-8119177 obtained from M.fortuitum ATCC 6842. Furthermore, Mycobacterium fortuitum NRRL-B-12433178, a double mutant obtained from M. fortuitum NRRL-B-8119, is able to partially degrade the side chain of sitosterol (7), with concomitant 9a-hydroxylation, to give the pregnadiene-20-carboxylic acid 8. 

The stereoselective hydrolysis of D,L-N-carbamoyl-methionine by the use of micro-oiganisms of the type Agrobacterium rhizogenes IFO 13259, Coiynebacterium sepedonicum IFO 3306, and Mycobacterium smegmatics ATCC 607, producing L-medtionine and D-N-caibamoyl-metiiionine, has so been described. 

As a biocatalyst that is capable of converting a,a-disubstituted amino acids efficiently, an aminopeptidase in the strain Mycobacterium neoaurum [ATCC 25795]... 

Permeabilized whole cells of Mycobacterium neoaurum ATCC 25795 or crude enzyme preparations can be used. 

Polyether antibiotic Staph, aureus ATCC No. 6538P Sarcina lutea 9341 Bacillus sp. E 27859 Bacillus suhtilis 558b Bacillus megaterium 8011 Bacillus sp. TA 27860 Mycobacterium phlei 355 Streptomyces cellulosae 3313 Paecilomyces varioti 26820... 

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... 

In general higher PCMC concentrations are necessary to achieve a bactericidal effect against mycobacteria, e.g. 1500-5000 ppm for Mycobacterium tuberculosis ATCC 25618. 

Escherichia coli EHEC DSM 8579 Legionella pneumophila ATCC 33152 Leuconostoc mesenteroides Listeria monocytogenes DSM 20600 Mycobacterium terrae DSM 43227 Propionibacterium acnes DSM 20458 Proteus mirabilis Pseudomonas aeruginosa Pseudomonas fluorescens Salmonella choleraesuis DSM 4224 Staphylococcus aureus MUSA Staphylococcus aureus MRSA DSM 2569... 

Mycobacterium tuberculosis Multiresistant strain of M. tuberculosis M. smegmatis ATCC 14468... 

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

Identically to the enz5miatic resolution process for a-H-amino acid amides by P. putida, we searched for a new biocatalyst for the stereoselective hydrolysis of a,a-disub-stituted amino acid amides (15). Through screening a new biocatalyst Mycobacterium neoaurum ATCC 25795 was obtained that fulfilled the demand for stereoselective hydrolysis [43,44]. 

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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