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<b>Abstract</b>— <p>A new flavoenzyme, HpnW from the soil organophosphonate (OP) degrader <i>Achromobacter insolitus</i> Kg 19 was isolated and characterized. Methods of determining HpnW activity in conjugated reactions with horseradish peroxidase or recombinant phosphonatase were developed. It was demonstrated that the&#xa0;enzyme performs oxidative deamination of 2-aminoethylphosphonic acid (2-AEP) producing phosphonoacetaldehyde, but is unable to attack other OPs, including the herbicide glyphosate. The main kinetic characteristics of HpnW were established to be as follows: <i>K</i><sub>m</sub> = 1.56 mM, <i>V</i><sub>maх</sub> = 0.70 U/mg of protein, <i>k</i><sub>cat</sub>&#xa0;= 0.47&#xa0;s<sup>–1</sup><sub>.</sub> With 2-AEP as the substrate, the <i>A. insolitus</i> Kg 19 enzyme exhibited higher catalytic efficiency compared to a number of homologs described in the literature but was significantly less active than the <i>Mariniblastus fucicola</i> PbfD2 oxidase. The reaction under study was inhibited by Cu<sup>2+</sup> and Ag<sup>+</sup> ions, as well as by glyphosate and aminomethylphosphonate. It was established that the enzyme preparation could be stored for a long time in a buffer with a high ionic strength in the presence of glycerol.</p>

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A Novel Flavin Oxidase as a Part of Phosphonatase Metabolic Pathway in Soil Organophosphonate-Degrading Bacteria Achromobacter insolitus

  • 期刊论文

  • 发表日期：

    2026年5月25日

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  • A. V. Sviridov,
  • D. O. Epiktetov,
  • S. V. Tarlachkov,
  • T. V. Shushkova,
  • A. A. Leontievsky

摘要

Abstract—

A new flavoenzyme, HpnW from the soil organophosphonate (OP) degrader Achromobacter insolitus Kg 19 was isolated and characterized. Methods of determining HpnW activity in conjugated reactions with horseradish peroxidase or recombinant phosphonatase were developed. It was demonstrated that the enzyme performs oxidative deamination of 2-aminoethylphosphonic acid (2-AEP) producing phosphonoacetaldehyde, but is unable to attack other OPs, including the herbicide glyphosate. The main kinetic characteristics of HpnW were established to be as follows: Km = 1.56 mM, Vmaх = 0.70 U/mg of protein, kcat = 0.47 s–1. With 2-AEP as the substrate, the A. insolitus Kg 19 enzyme exhibited higher catalytic efficiency compared to a number of homologs described in the literature but was significantly less active than the Mariniblastus fucicola PbfD2 oxidase. The reaction under study was inhibited by Cu2+ and Ag+ ions, as well as by glyphosate and aminomethylphosphonate. It was established that the enzyme preparation could be stored for a long time in a buffer with a high ionic strength in the presence of glycerol.