The <i>β</i>‐cyanoalanine synthase pathway: beyond cyanide detoxification

Machingura, Marylou; Salomon, Eitan; Jez, Joseph M.; Ebbs, Stephen D.

doi:10.1111/pce.12755

Cited by 75 publications

(54 citation statements)

References 187 publications

(387 reference statements)

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“…Even without β‐CAS activity, quinclorac tolerance level remained extremely high in the mutant rice. The slight activity detected in the knockout rice mutant could be explained by cytosolic O ‐acetylserine sulfhydrylase in our enzyme extract . These results are in agreement with the recent findings that β‐CAS is not involved in quinclorac resistance in Echinochloa spp .…”

Section: Discussionsupporting

confidence: 93%

Quinclorac resistance in Echinochloa phyllopogon is associated with reduced ethylene synthesis rather than enhanced cyanide detoxification by β‐cyanoalanine synthase

Chayapakdee

Sunohara

Endo

et al. 2019

Pest Management Science

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BACKGROUND Multiple herbicide resistant Echinochloa phyllopogon exhibits resistance to the auxin herbicide quinclorac. Previous research observed enhanced activity of the cyanide‐detoxifying enzyme β‐cyanoalanine synthase (β‐CAS) and reduced ethylene production in the resistant line, suggesting β‐CAS‐mediated cyanide detoxification and insensitivity to quinclorac stimulation as the resistance mechanisms. To investigate the molecular mechanisms of quinclorac resistance, we characterized the β‐CAS genes alongside plant transformation studies. The association of β‐CAS activity and ethylene production to quinclorac resistance was assayed in the F6 progeny of susceptible and resistant lines of E. phyllopogon. RESULTS A single nucleotide polymorphism in a β‐CAS1 intron deleted aberrantly spliced mRNAs and enhanced β‐CAS activity in the resistant line. The enhanced activity, however, was not associated with quinclorac resistance in F6 lines. The results were supported by lack of quinclorac resistance in Arabidopsis thaliana expressing E. phyllopogon β‐CAS1 and no difference in quinclorac sensitivity between β‐CAS knockout and wild‐type rice. Reduced ethylene production co‐segregated with quinclorac resistance in F6 lines which were previously characterized to be resistant to other herbicides by an enhanced metabolism. CONCLUSION β‐CAS does not participate in quinclorac sensitivity in E. phyllopogon. Our results suggest that a mechanism(s) leading to reduced ethylene production is behind the resistance. © 2019 Society of Chemical Industry

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Section: Discussionsupporting

confidence: 93%

Quinclorac resistance in Echinochloa phyllopogon is associated with reduced ethylene synthesis rather than enhanced cyanide detoxification by β‐cyanoalanine synthase

Chayapakdee

Sunohara

Endo

et al. 2019

Pest Management Science

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“…It should be noted that the observed variation in the cyanogenic glucosides is not always related to the content of the cyano‐amino acid compounds, despite their biochemical link. In plants, cyanide (CN − ) is a naturally occurring molecule produced through biological and environmental processes and this metabolic poison requires detoxification (Machingura, Salomon, Jez, & Ebbs, ; Yi et al, ). The cyanide in higher plants is produced by several catabolic reactions, such as the biosynthesis of ethylene, degradation of cyanogenic glycosides, glucosinolates, the oxidation of amino acids and the metabolism of hydroxylamine (Sánchez‐Pérez, Jørgensen, Motawia, Dicenta, & Møller, ).…”

Section: Discussionmentioning

confidence: 99%

Polymorphisms in cyanogenic glucoside and cyano‐amino acid content in natural accessions of common vetch (Vicia sativa L.) and selection for improved agronomic performance

et al. 2019

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Common vetch (Vicia sativa L.) is an important annual forage legume. It is used as a cover crop, green manure, pasture legume and for silage and hay production. Its seeds can be used as a source of highly digestible protein and minerals in animal diets. However, their utilization as a feedstuff for monogastric animals is hindered by the fact that the seeds contain cyanogenic antinutritional factors that reduce their palatability. An effective utilization of V. sativa seeds as a successful monogastric feed stuff requires selection for higher protein availability and minimization of the cyanogenic antinutritional factors content. In this study, we selected one natural accession named Mjez Ibeb, from a collection of 25 accessions and cultivars, based on its superior agronomic performance and its naturally occurring genetic variation for cyanogenic traits. We investigated the genetic variation that exists for the cyanogenesis trait in more detail and analysed the seeds of 133 lines derived from accession Mjez lbeb. Of these, 40 naturally polymorphic lines that showed deficiencies in cyanogenesis and cyano‐amino acid content, were subsequently selected for detailed chemical analysis. Cyanogenic glucosides and cyano‐amino acid concentrations varied widely in the 40 lines. Multivariate analysis was performed and three lines (L16, L21, L18) with low content of cyanogenic compounds were identified.

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“…In cysteine biosynthesis, CS catalyzes cysteine formation from O-acetylserine and hydrogen sulfide. Cysteine is then used as a substrate for CAS in the detoxification of cyanide in plants [48]. Subsequent conversion of β-cyanoalanine to asparagine leads to the generation of isoxazolin-5-one.…”

Section: β-Odap Biosynthesis In Grass Peamentioning

confidence: 99%

“…Cyanide (CN − is a naturally occurring molecule in plants and is produced during ethylene biosynthesis [48]. It also acts as a signaling molecule in regulating metabolic processes like seed germination and dormancy release [68], and plays a role in resistance to biotic and abiotic stresses [69,70].…”

Section: β-Cyanoalanine Synthase (Cas) and Cyanide Detoxification mentioning

confidence: 99%

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β-N-Oxalyl-l-α,β-diaminopropionic Acid (β-ODAP) Content in Lathyrus sativus: The Integration of Nitrogen and Sulfur Metabolism through β-Cyanoalanine Synthase

Liu

Chen

et al. 2017

IJMS

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Grass pea (Lathyrus sativus L.) is an important legume crop grown mainly in South Asia and Sub-Saharan Africa. This underutilized legume can withstand harsh environmental conditions including drought and flooding. During drought-induced famines, this protein-rich legume serves as a food source for poor farmers when other crops fail under harsh environmental conditions; however, its use is limited because of the presence of an endogenous neurotoxic nonprotein amino acid β-N-oxalyl-l-α,β-diaminopropionic acid (β-ODAP). Long-term consumption of Lathyrus and β-ODAP is linked to lathyrism, which is a degenerative motor neuron syndrome. Pharmacological studies indicate that nutritional deficiencies in methionine and cysteine may aggravate the neurotoxicity of β-ODAP. The biosynthetic pathway leading to the production of β-ODAP is poorly understood, but is linked to sulfur metabolism. To date, only a limited number of studies have been conducted in grass pea on the sulfur assimilatory enzymes and how these enzymes regulate the biosynthesis of β-ODAP. Here, we review the current knowledge on the role of sulfur metabolism in grass pea and its contribution to β-ODAP biosynthesis. Unraveling the fundamental steps and regulation of β-ODAP biosynthesis in grass pea will be vital for the development of improved varieties of this underutilized legume.

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The β‐cyanoalanine synthase pathway: beyond cyanide detoxification

Cited by 75 publications

References 187 publications

Quinclorac resistance in Echinochloa phyllopogon is associated with reduced ethylene synthesis rather than enhanced cyanide detoxification by β‐cyanoalanine synthase

Quinclorac resistance in Echinochloa phyllopogon is associated with reduced ethylene synthesis rather than enhanced cyanide detoxification by β‐cyanoalanine synthase

Polymorphisms in cyanogenic glucoside and cyano‐amino acid content in natural accessions of common vetch (Vicia sativa L.) and selection for improved agronomic performance

β-N-Oxalyl-l-α,β-diaminopropionic Acid (β-ODAP) Content in Lathyrus sativus: The Integration of Nitrogen and Sulfur Metabolism through β-Cyanoalanine Synthase

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