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Catalytic properties of aminoacylase of strain Rhodococcus armeniensis AM6.1

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Abstract

Studies of substrate specificity revealed that the D-aminoacylase of Rhodococcus armeniensis AM6.1 strain exhibits absolute stereospecificity to the D-stereoisomers of N-acetyl-amino acids. The enzyme is the most active reacted with N-acetyl-D-methionine, as well as with aromatic and hydrophobic N-acetylamino acids and interacts weakly with the basic substrates. It is practically not reacted with acidic and hydrophilic N-acetyl-amino acids. Michaelis constants (K m) and maximum reaction velocities (V max) were calculated, using linear regression analysis, for the following substrates: N-acetyl-D-methionine, N-acetyl-D-alanine, N-acetyl-D-phenylalanine, N-acetyl-D-tyrosine, N-acetyl-D-valine, N-acetyl-D-oxyvaline, N-acetyl- D-leucine. Substrate inhibition of D-aminoacylase was displayed with N-acetyl-D-leucine (K s = 35.5 ± 28.3 mM) and N-acetyl-DL-tyrosine (K s = 15.8 ± 4.5 mM). Competitive inhibition of the enzyme with product–acetic acid (K i = 104.7 ± 21.7 mM, K m = 2.5 ± 0.5 mM, V max = 25.1 ± 1.5 U/mg) was observed.

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Authors and Affiliations

  1. SPC “Armbiotechnology” NAS RA, Yerevan, 0056, Armenia

    A. A. Hambardzumyan, A. V. Mkhitaryan, A. M. Paloyan, S. A. Dadayan & A. S. Saghyan

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  1. A. A. Hambardzumyan
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  2. A. V. Mkhitaryan
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  3. A. M. Paloyan
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  4. S. A. Dadayan
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  5. A. S. Saghyan
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Correspondence to A. A. Hambardzumyan.

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Original Russian Text © A.A. Hambardzumyan, A.V. Mkhitaryan, A.M. Paloyan, S.A. Dadayan, A.S. Saghyan, 2016, published in Prikladnaya Biokhimiya i Mikrobiologiya, 2016, Vol. 52, No. 3, pp. 272–278.

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Hambardzumyan, A.A., Mkhitaryan, A.V., Paloyan, A.M. et al. Catalytic properties of aminoacylase of strain Rhodococcus armeniensis AM6.1. Appl Biochem Microbiol 52, 250–255 (2016). https://doi.org/10.1134/S0003683816030029

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  • DOI: https://doi.org/10.1134/S0003683816030029

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