ArticleThe Journal of biological chemistry2022
Identification and characterization of the key enzyme in the biosynthesis of the neurotoxin β-ODAP in grass pea.
Article in The Journal of biological chemistry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 21 citations in OpenAlex.
- Article
- CRISPR-Based genome editing in pulses: current approaches, challenges, and future prospects.Plant molecular biology · 2025Review
- Evaluation of genetic diversity and elucidation of population structure of Lathyrus accessions using agro-morphological characters and ISSR technique.Journal, genetic engineering & biotechnology · 2025Article
- Genome editing of an oxalyl-CoA synthetase gene in Lathyrus sativus reveals its role in oxalate metabolism.Plant cell reports · 2024Article
- The Potential of CRISPR/Cas9 to Circumvent the Risk Factor NeurotoxinCurrent issues in molecular biology · 2024Review
- Reply to: LsBOS utilizes oxalyl-CoA produced by LsAAE3 to synthesize β-ODAP in grass pea.Nature communications · 2024Article
- LsBOS utilizes oxalyl-CoA produced by LsAAE3 to synthesize β-ODAP in grass pea.Nature communications · 2024Article
- Genomics and biochemical analyses reveal a metabolon key to β-L-ODAP biosynthesis in Lathyrus sativus.Nature communications · 2023Article
- Exploiting genetic and genomic resources to enhance productivity and abiotic stress adaptation of underutilized pulses.Frontiers in genetics · 2023Review
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Authors and funding
14 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Grass pea (Lathyrus sativus L.) is a grain legume commonly grown in Asia and Africa for food and forage. It is a highly nutritious and robust crop, capable of surviving both droughts and floods. However, it produces a neurotoxic compound, β-N-oxalyl-L-α,β-diaminopropionic acid (β-ODAP), which can cause a severe neurological disorder when consumed as a primary diet component. While the catalytic activity associated with β-ODAP formation was demonstrated more than 50 years ago, the enzyme responsible for this activity has not been identified. Here, we report on the identity, activity, 3D structure, and phylogenesis of this enzyme-β-ODAP synthase (BOS). We show that BOS belongs to the benzylalcohol O-acetyltransferase, anthocyanin O-hydroxycinnamoyltransferase, anthranilate N-hydroxycinnamoyl/benzoyltransferase, deacetylvindoline 4-O-acetyltransferase superfamily of acyltransferases and is structurally similar to hydroxycinnamoyl transferase. Using molecular docking, we propose a mechanism for its catalytic activity, and using heterologous expression in tobacco leaves (Nicotiana benthamiana), we demonstrate that expression of BOS in the presence of its substrates is sufficient for β-ODAP production in vivo. The identification of BOS may pave the way toward engineering β-ODAP-free grass pea cultivars, which are safe for human and animal consumption.
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