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IUBMB CommentsThe enzyme, characterized from the bacterium Ochrobactrum sp. G-1, contains an FAD cofactor. The catalytic cycle starts with a reduction of the FAD cofactor by one molecule of glyphosate, yielding reduced FAD and a Schiff base of aminomethylphosphonate with glyoxylate that is hydrolysed to the single components. The reduced FAD is reoxidized by oxygen, generating water and an oxygenated flavin intermediate, which catalyses the oxygenation of a second molecule of glyphosate, forming the second pair of aminomethylphosphonate and glyoxylate.
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2 glyphosate + O2
2 aminomethylphosphonate + 2 glyoxylate
2 glyphosate + O2
2 aminomethylphosphonate + 2 glyoxylate
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2 glyphosate + O2
2 aminomethylphosphonate + 2 glyoxylate
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glyphosate concentration decreases with an equimolar increase of the concentrations of aminomethylphosphonate and glyoxylate
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2 glyphosate + O2
2 aminomethylphosphonate + 2 glyoxylate
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glyphosate concentration decreases with an equimolar increase of the concentrations of aminomethylphosphonate and glyoxylate
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2 glyphosate + O2
2 aminomethylphosphonate + 2 glyoxylate
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2 glyphosate + O2
2 aminomethylphosphonate + 2 glyoxylate
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2 glyphosate + O2
2 aminomethylphosphonate + 2 glyoxylate
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metabolism
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strain CB4 degrades glyphosate along two concurrent pathways to aminomethylphosphonate, glyoxylate, sarcosine, glycine and formaldehyde as products, i.e. by the C-P lyase activity and the glyphosate oxidoreductase activity
metabolism
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strain CB4 degrades glyphosate along two concurrent pathways to aminomethylphosphonate, glyoxylate, sarcosine, glycine and formaldehyde as products, i.e. by the C-P lyase activity and the glyphosate oxidoreductase activity
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physiological function
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a rapid decrease of the concentration of aminomethylphosphonate resulting from the glyphospate cleavage is observed in the presence of pyridoxal 5'-phosphate and pyruvate. aminomethylphosphonate: pyruvate aminotransferase, is the second enzyme of the proposed phosphonatase pathway of glyphosate transformation. Glyphospate metabolism in Ochrobactrum anthropi GPK 3 is accompanied by intracellular formation of formaldehyde
physiological function
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Geobacillus caldoxylosilyticus is able to utilize a number of organophosphonates as the sole phosphorus source for growth at 60°C. During growth on glyphosate, aminomethylphosphonate release to the medium is observed
physiological function
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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
physiological function
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in Ochrobactrum sp., glyphosate (3 mM) degradation is induced by phosphate starvation, and is completed within 60 h. Aminomethylphosphonic acid is detected in the exhausted medium. The bacterium grows even in the presence of glyphosate concentrations as high as 200 mM
physiological function
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Geobacillus caldoxylosilyticus is able to utilize a number of organophosphonates as the sole phosphorus source for growth at 60°C. During growth on glyphosate, aminomethylphosphonate release to the medium is observed
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physiological function
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a rapid decrease of the concentration of aminomethylphosphonate resulting from the glyphospate cleavage is observed in the presence of pyridoxal 5'-phosphate and pyruvate. aminomethylphosphonate: pyruvate aminotransferase, is the second enzyme of the proposed phosphonatase pathway of glyphosate transformation. Glyphospate metabolism in Ochrobactrum anthropi GPK 3 is accompanied by intracellular formation of formaldehyde
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physiological function
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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
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analysis
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spectrophotometric method for determining glyphospate oxidoreductase activity in cell-free extract based on the rate of glyoxylate hydrazone formation
analysis
use of quantitative competitive PCR to estimate the copy number of the synthetic gox gene as a transgene, and measure of its transcript levels in transformed canola lines. There is no direct relationship between copy number and gene expression level for the gene
analysis
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spectrophotometric method for determining glyphospate oxidoreductase activity in cell-free extract based on the rate of glyoxylate hydrazone formation
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degradation
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in Ochrobactrum sp., glyphosate (3 mM) degradation is induced by phosphate starvation, and is completed within 60 h. The bacterium grows even in the presence of glyphosate concentrations as high as 200 mM
degradation
Pseudomonas spp.
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inoculating glyphosate-treated soil samples with Pseudomonas sp. strains GA07, GA09 and GC04 results in a 2-3 times higher rate of glyphosate removal than that in non-inoculated soil. The degradation kinetics follows a first-order model. Glyphosate breakdown in strain GA09 is catalyzed both by C-P lyase and glyphosate oxidoreductase. Strains GA07 and GC04 degrade glyphosate only via glyphosate oxidoreductase, but no further metabolite is detected
degradation
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upon cultivation at initial pH 6.0, incubation temperature 35°C, glyphosate concentration 6 g/l, inoculation amount 5% and incubation time 5 days, strain CB4 utilizes 94.47% of glyphosate. The strain degrades glyphosate concentrations up to 12 g/l
degradation
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upon cultivation at initial pH 6.0, incubation temperature 35°C, glyphosate concentration 6 g/l, inoculation amount 5% and incubation time 5 days, strain CB4 utilizes 94.47% of glyphosate. The strain degrades glyphosate concentrations up to 12 g/l
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Obojska, A.; Ternan, N.G.; Lejczak, B.; Kafarski, P.; McMullan, G.
Organophosphonate utilization by the thermophile Geobacillus caldoxylosilyticus T20
Appl. Environ. Microbiol.
68
2081-2084
2002
Parageobacillus caldoxylosilyticus, Parageobacillus caldoxylosilyticus T20
brenda
Sviridov, A.V.; Shushkova, T.V.; Zelenkova, N.F.; Vinokurova, N.G.; Morgunov, I.G.; Ermakova, I.T.; Leontievsky, A.A.
Distribution of glyphosate and methylphosphonate catabolism systems in soil bacteria Ochrobactrum anthropi and Achromobacter sp.
Appl. Microbiol. Biotechnol.
93
787-796
2012
Brucella anthropi, Brucella anthropi GPK 3
brenda
Sviridov, A.V.; Zelenkova, N.F.; Vinokurova, N.G.; Ermakova, I.T.; Leontievsky, A.A.
New approaches to identification and activity estimation of glyphosate degradation enzymes
Biochemistry (Moscow)
76
720-725
2011
Brucella anthropi, Brucella anthropi GPK 3
brenda
Hadi, F.; Salmanian, A.; Mousavi, A.; Ghazizadeh, E.; Amani, J.; Noghabi, K.
Development of quantitative competitive PCR for determination of copy number and expression level of the synthetic glyphosate oxidoreductase gene in transgenic canola plants
Electron. J. Biotechnol.
15
2
2012
Ochrobactrum sp. G-1 (D2KI28)
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brenda
Hadi, F.; Mousavi, A.; Noghabi, K.; Tabar, H.; Salmanian, A.
New bacterial strain of the genus Ochrobactrum with glyphosate-degrading activity
J. Environ. Sci. Health B
48
208-213
2013
Ochrobactrum sp. GDOS
brenda
Fan, J.; Yang, G.; Zhao, H.; Shi, G.; Geng, Y.; Hou, T.; Tao, K.
Isolation, identification and characterization of a glyphosate-degrading bacterium, Bacillus cereus CB4, from soil
J. Gen. Appl. Microbiol.
58
263-271
2012
Bacillus cereus, Bacillus cereus CB4
brenda
Zhao, H.; Tao, K.; Zhu, J.; Liu, S.; Gao, H.; Zhou, X.
Bioremediation potential of glyphosate-degrading Pseudomonas spp. strains isolated from contaminated soil
J. Gen. Appl. Microbiol.
61
165-170
2015
Pseudomonas spp.
brenda
Bhatt, P.; Joshi, T.; Bhatt, K.; Zhang, W.; Huang, Y.; Chen, S.
Binding interaction of glyphosate with glyphosate oxidoreductase and C-P lyase Molecular docking and molecular dynamics simulation studies
J. Hazard. Mater.
409
124927
2021
Ochrobactrum sp. G-1 (D2KI28)
brenda
1.5.3.23 glyphosate oxidoreductase
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