Kinetic Traits and Enzyme Form Patterns of <i>(R)</i>‐2‐(2,4‐Dichlorophenoxy)propionate/α‐Ketoglutarate Dioxygenase (RdpA) after Expression in Different Bacterial Strains

Westendorf, A.; Benndorf, Dirk; Pribýl, T; Harms, Hauke; Müller, Roland

doi:10.1002/elsc.200620165

Cited by 14 publications

(23 citation statements)

References 27 publications

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“…In addition, they are characterized by very fast adaptation to a given cultivation technique. The weeds collected during harvest can also carry bacterial, viral or fungal diseases, and can thus be harmful to humans and animals . Therefore application of herbicides is a common necessity with no other alternative.…”

Section: Introductionmentioning

confidence: 99%

Herbicidal Ionic Liquids Containing the Acetylcholine Cation

et al. 2019

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This study presents a new group of herbicidal ionic liquids (HILs) based on a cation occurs commonly in nature−acetylcholine. The HILs were obtained with a high yield through ion exchange between acetylcholine chloride and potassium or sodium salts of selected acids with herbicidal activity. The results of the herbicidal activity measurement against common oilseed rape (Brassica napus L.) exceeded those of the commercial products. Spray solutions of the synthesized HILs revealed high surface activity and wetting properties which further manifested as higher herbicidal activity. The reduction of surface tension and low contact angles together with the specific action of acetylcholine allowed for better penetration of synthesized HILs into plant tissues. In addition, OECD 301F tests confirmed high mineralization of the HILs. The simple transformation of commercial herbicides into acetylcholine HILs proved to be a very effective method of increasing their activity, and constitutes an interesting solution to the problem of weed infestation with the use of a substance commonly found in nature.

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Section: Introductionmentioning

confidence: 99%

Herbicidal Ionic Liquids Containing the Acetylcholine Cation

et al. 2019

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“…The best described are Sphingomonas herbicidovorans MH (16,48) and Delftia acidovorans MC1 (28,29), from which rdpA and sdpA genes were first isolated and sequenced (30,39). Enzyme activity from these strains has shown that RdpA dioxygenase is generally highly specific to the R enantiomer of 2-phenoxypropionates and shows very weak activity toward phenoxyacetates, whereas SdpA is enantioselective to the S enantiomer but can also convert certain phenoxyacetates such as 2,4-D and MCPA with various catalytic activities (27,31,44,45). The genetic background has only recently become available and shows that rdpA sequences reported to date are nearly identical while sdpA sequences between S. herbicidovorans MH and D. acidovorans MC1 are far more variable (30,39).…”

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confidence: 99%

Abundance and Expression of Enantioselective rdpA and sdpA Dioxygenase Genes during Degradation of the Racemic Herbicide ( R , S )-2-(2,4-Dichlorophenoxy)Propionate in Soil

Paulin

Nicolaisen

Sørensen

2010

Appl Environ Microbiol

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The rdpA and sdpA genes encode two enantioselective ␣-ketoglutarate-dependent dioxygenases catalyzing the initial step of microbial degradation of the chiral herbicide (R,S)-2-(2,4-dichlorophenoxy)propionate (R,Sdichlorprop). Primers were designed to assess abundance and transcription dynamics of rdpA and sdpA genes in a natural agricultural soil. No indigenous rdpA genes were detected, but sdpA genes were present at levels of approximately 10 3 copies g of soil ؊1 . Cloning and sequencing of partial sdpA genes revealed a high diversity within the natural sdpA gene pool that could be divided into four clusters by phylogenetic analysis. BLASTp analysis of deduced amino acids revealed that members of cluster I shared 68 to 69% identity, cluster II shared 78 to 85% identity, cluster III shared 58 to 64% identity, and cluster IV shared 55% identity to their closest SdpA relative in GenBank. Expression of rdpA and sdpA in Delftia acidovorans MC1 inoculated in soil was monitored by reverse transcription quantitative real-time PCR (qPCR) during in situ degradation of 2 and 50 mg kg ؊1 of (R,S)-dichlorprop. (R,S)-Dichlorprop amendment created a clear upregulation of both rdpA and sdpA gene expression during the active phase of 14 C-labeled (R,S)-dichlorprop mineralization, particularly following the second dose of 50 mg kg ؊1 herbicide. Expression of both genes was maintained at a low constitutive level in nonamended soil microcosms. This study is the first to report the presence of indigenous sdpA genes recovered directly from natural soil and also comprises the first investigation into the transcription dynamics of two enantioselective dioxygenase genes during the in situ degradation of the herbicide (R,S)-dichlorprop in soil.

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“…The basal 2,4-D consumption (Tables 1 and 2) can be explained by some catalytic activity of RdpA with 2,4-D [5,10] and consequently wash-in of 2,4-D into chemostat cultures growing on (R)-2,4-DP proceeded to stationary 2,4-D concentrations well below those in the feeding solution (Fig. 1).…”

Section: Adaptation Resulting In Faster 24-d Degradationmentioning

confidence: 94%

“…P230 were 2-5 times lower for all phenoxyalkanoates than those of RdpA derived from the other two strains. Moreover, the K m values of strain P230 for phenoxyacetates were more similar to those for (R)-phenoxypropionates [10]. These differences correlated with the appearance of multiple forms of RdpA, resulting from posttranslational modification, which became visible after separation in 2D gels [10,11].…”

Section: Introductionmentioning

confidence: 84%

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Posttranslational oxidative modification of (R)‐2‐(2,4‐dichlorophenoxy)propionate/α‐ketoglutarate‐dependent dioxygenases (RdpA) leads to improved degradation of 2,4‐dichlorophenoxyacetate (2,4‐D)

Leibeling

Maess

Centler

et al. 2013

Engineering in Life Sciences

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Microbial activities and the versatility gained through adaptation to xenobiotic compounds are the main biological forces to counteract environmental pollution.The current results present a new adaptive mechanism that is mediated through posttranslational modifications. Strains of Delftia acidovorans incapable of growing autochthonously on 2,4-dichlorophenoxyacetate (2,4-D) were cultivated in a chemostat on 2,4-D in the presence of (R)-2-(2,4-dichlorophenoxy)propionate. Long-term cultivation led to enhanced 2,4-D degradation, as demonstrated by improved values of the Michaelis-Menten constant K m for 2,4-D and the catalytic efficiency k cat /K m of the initial degradative key enzyme (R)-2-(2,4-dichlorophenoxy)propionate/ α-ketoglutarate-dependent dioxygenases (RdpA). Analyses of the rdpA gene did not reveal any mutations, indicating a nongenetic mechanism of adaptation. 2-DE of enzyme preparations, however, showed a series of RdpA forms varying in their pI. During adaptation increased numbers of RdpA variants were observed. Subsequent immunoassays of the RdpA variants showed a specific reaction with 2,4-dinitrophenylhydrazine (DNPH), characteristic of carbonylation modifications. Together these results indicate that posttranslational carbonylation modified the substrate specificity of RdpA. A model was implemented explaining the segregation of clones with improved degradative activity within the chemostat. The process described is capable of quickly responding to environmental conditions by reversibly adapting the degradative potential to various phenoxyalkanoate herbicides.Keywords: 2,4-Dichlorophenoxyacetate (2,4-D) / (R)-2-(2,4-Dichlorophenoxy)propionate / α-ketoglutarate-dependent dioxygenases (RdpA) / Individual-based modeling / Posttranslational carbonylationAdditional supporting information may be found in the online version of this article at the publisher's web-site

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Kinetic Traits and Enzyme Form Patterns of (R)‐2‐(2,4‐Dichlorophenoxy)propionate/α‐Ketoglutarate Dioxygenase (RdpA) after Expression in Different Bacterial Strains

Cited by 14 publications

References 27 publications

Herbicidal Ionic Liquids Containing the Acetylcholine Cation

Herbicidal Ionic Liquids Containing the Acetylcholine Cation

Abundance and Expression of Enantioselective rdpA and sdpA Dioxygenase Genes during Degradation of the Racemic Herbicide ( R , S )-2-(2,4-Dichlorophenoxy)Propionate in Soil

Posttranslational oxidative modification of (R)‐2‐(2,4‐dichlorophenoxy)propionate/α‐ketoglutarate‐dependent dioxygenases (RdpA) leads to improved degradation of 2,4‐dichlorophenoxyacetate (2,4‐D)

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