A new aliphatic amidase gene (ami), having a less than 77% level of similarity with the nearest homologs, was identified in the Rhodococcus erythropolis TA37 strain, which is able to hydrolyze a wide range of amides. The amidase gene was cloned within a 3.7 kb chromosomal locus, which also contains putative acetyl-CoA ligase and ABC-type transporter genes. The structure of this locus in the R. erythropolis TA37 strain differs from the structure of loci in other Rhodococcus strains. The amidase gene is expressed in Escherichia coli cells. It was demonstrated that amidase (generated in the recombinant strain) efficiently hydrolyzes acetamide (aliphatic amide) and does not use 4′-nitroacetanilide (N-substituted amide) as a substrate. Insertional inactivation of the amidase gene in the R. erythropolis TA37 strain results in a considerable decrease (by at least 6–7 times) in basal amidase activity, indicating functional amidase activity in the R. erythropolis TA37 strain.
Russian Journal of Genetics – Springer Journals
Published: Oct 23, 2014
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