Overproduction and characterization of the first enzyme of a new aldoxime dehydratase family in Bradyrhizobium sp.

Rädisch, Robert; Chmátal, Martin; Rucká, Lenka; Novotný, Petr; Petrásková, Lucie; Halada, Petr; Kotik, Michael; Pátek, Miroslav; Martı́nková, Ludmila

doi:10.1016/j.ijbiomac.2018.04.103

Cited by 21 publications

(16 citation statements)

References 35 publications

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“…The Oxds of Rhodococcus are ≈76% identical to those of Pseudomonas , but those of Bradyrhizobium sp. [ 24 ] and Bacillus sp. [ 25 ] are more distant with ≈47% and ≈32% identity, respectively.…”

Section: Substrate Specificitymentioning

confidence: 99%

“…OxdBr1 of Bradyrhizobium sp. LTSPM299 was found to be similar to OxdB and OxdRG in terms of substrate specificity [ 24 ]. The Oxd of Rhododoccus sp.…”

Section: Substrate Specificitymentioning

confidence: 99%

“…Two hypothetical genes were found upstream of the oxd gene in Bacillus and Brady-rhizobium [ 23 , 24 ]. They probably encode an NLase and a transcriptional regulator NitR, which belongs to the AraC family.…”

Section: Substrate Specificitymentioning

confidence: 99%

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Metabolism of Aldoximes and Nitriles in Plant-Associated Bacteria and Its Potential in Plant-Bacteria Interactions

et al. 2022

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In plants, aldoximes per se act as defense compounds and are precursors of complex defense compounds such as cyanogenic glucosides and glucosinolates. Bacteria rarely produce aldoximes, but some are able to transform them by aldoxime dehydratase (Oxd), followed by nitrilase (NLase) or nitrile hydratase (NHase) catalyzed transformations. Oxds are often encoded together with NLases or NHases in a single operon, forming the aldoxime–nitrile pathway. Previous reviews have largely focused on the use of Oxds and NLases or NHases in organic synthesis. In contrast, the focus of this review is on the contribution of these enzymes to plant-bacteria interactions. Therefore, we summarize the substrate specificities of the enzymes for plant compounds. We also analyze the taxonomic and ecological distribution of the enzymes. In addition, we discuss their importance in selected plant symbionts. The data show that Oxds, NLases, and NHases are abundant in Actinobacteria and Proteobacteria. The enzymes seem to be important for breaking through plant defenses and utilizing oximes or nitriles as nutrients. They may also contribute, e.g., to the synthesis of the phytohormone indole-3-acetic acid. We conclude that the bacterial and plant metabolism of aldoximes and nitriles may interfere in several ways. However, further in vitro and in vivo studies are needed to better understand this underexplored aspect of plant–bacteria interactions.

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Section: Substrate Specificitymentioning

confidence: 99%

“…OxdBr1 of Bradyrhizobium sp. LTSPM299 was found to be similar to OxdB and OxdRG in terms of substrate specificity [ 24 ]. The Oxd of Rhododoccus sp.…”

Section: Substrate Specificitymentioning

confidence: 99%

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Metabolism of Aldoximes and Nitriles in Plant-Associated Bacteria and Its Potential in Plant-Bacteria Interactions

et al. 2022

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“…The Oxd (EC 4.99.1.5-7) in this reaction sequence is a heme-protein that catalyzes oxime dehydration. Oxds were found in the bacteria Rhodococcus, Pseudomonas, Bradyrhizobium and in fungi (Fusarium, Sclerotinia) [13][14][15] and have been studied as catalysts for mild and sustainable nitrile synthesis. 16,17 Their biocatalytic potential lies in their ability to dehydrate oximes in an aqueous medium and thus produce nitriles in a cyanide-free fashion.…”

mentioning

confidence: 99%

“…LTSPM299 is an exception, since it does not require strictly anaerobic conditions. 15 This fact was important in light of the oxygen requirement of the CARcontaining living cell biocatalyst and rendered OxdBr1 a promising candidate for the cascade.…”

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confidence: 99%