New approaches to identification and activity estimation of glyphosate degradation enzymes

• Published in: Biochemistry (Moscow) Vol. 76; no. 6; pp. 720 - 725
• Main Authors: Sviridov, A. V., Zelenkova, N. F., Vinokurova, N. G., Ermakova, I. T., Leontievsky, A. A.
• Format: Journal Article
• Language: English
• Published: Dordrecht SP MAIK Nauka/Interperiodica 01.06.2011; Springer; Springer Nature B.V
• Subjects: Achromobacter; Achromobacter - enzymology; Amino acids; Analysis; Biochemistry; Biomedical and Life Sciences; Biomedicine; Bioorganic Chemistry; Chromatography; Chromatography, High Pressure Liquid; Enzymes; Glycine - analogs & derivatives; Glycine - metabolism; Glyphosate; Isoxazoles; Life Sciences; Liquid chromatography; Lyases - metabolism; Methods; Microbiology; Ochrobactrum anthropi - enzymology; Organophosphonates - metabolism; Oxidoreductases - metabolism; Physiological aspects; Sarcosine - metabolism; Tetrazoles; liquid chromatography; C-P lyase; glyphosate; thin layer chromatography; glyphosate-oxidoreductase
• ISSN: 0006-2979; 1608-3040
• DOI: 10.1134/S0006297911060149

We propose a new set of approaches, which allow identifying the primary enzymes of glyphosate (N-phosphonomethyl-glycine) attack, measuring their activities, and quantitative analysis of glyphosate degradation in vivo and in vitro . Using the developed approach we show that glyphosate degradation can follow different pathways depending on physiological characteristics of metabolizing strains: in Ochrobactrum anthropi GPK3 the initial cleavage reaction is catalyzed by glyphosate-oxidoreductase with the formation of aminomethylphosphonic acid and glyoxylate, whereas Achromobacter sp. MPS12 utilize C-P lyase, forming sarcosine. The proposed methodology has several advantages as compared to others described in the literature.