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231226s2023 xx |||||o 00| ||eng c |
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|a 10.1016/j.plaphy.2023.108127
|2 doi
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|a pubmed25n1212.xml
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|a (DE-627)NLM363822895
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|a (NLM)37890229
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|a (PII)S0981-9428(23)00638-1
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|a DE-627
|b ger
|c DE-627
|e rakwb
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|a eng
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|a Foletto-Felipe, Marcela de Paiva
|e verfasserin
|4 aut
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|a Inhibition of O-acetylserine (thiol) lyase as a promising new mechanism of action for herbicides
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|c 2023
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
|b c
|2 rdamedia
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|a ƒa Online-Ressource
|b cr
|2 rdacarrier
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|a Date Completed 28.11.2023
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|a Date Revised 28.11.2023
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a Copyright © 2023. Published by Elsevier Masson SAS.
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|a Enzymes of the sulfur assimilation pathway of plants have been identified as potential targets for herbicide development, given their crucial role in synthesizing amino acids, coenzymes, and various sulfated compounds. In this pathway, O-acetylserine (thiol) lyase (OAS-TL; EC 2.5.1.47) catalyzes the synthesis of L-cysteine through the incorporation of sulfate into O-acetylserine (OAS). This study used an in silico approach to select seven inhibitors for OAS-TL. The in silico experiments revealed that S-benzyl-L-cysteine (SBC) had a better docking score (-7.0 kcal mol-1) than the substrate OAS (-6.6 kcal mol-1), indicating its suitable interaction with the active site of the enzyme. In vitro experiments showed that SBC is a non-competitive inhibitor of OAS-TL from Arabidopsis thaliana expressed heterologously in Escherichia coli, with a Kic of 4.29 mM and a Kiu of 5.12 mM. When added to the nutrient solution, SBC inhibited the growth of maize and morning glory weed plants due to the reduction of L-cysteine synthesis. Remarkably, morning glory was more sensitive than maize. As proof of its mechanism of action, L-cysteine supplementation to the nutrient solution mitigated the inhibitory effect of SBC on the growth of morning glory. Taken together, our data suggest that reduced L-cysteine synthesis is the primary cause of growth inhibition in maize and morning glory plants exposed to SBC. Furthermore, our findings indicate that inhibiting OAS-TL could potentially be a novel approach for herbicidal action
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|a Journal Article
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|a Bioinformatics
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|a L-cysteine
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|a New herbicidal action site
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|a O-acetylserine (thiol) lyase
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|a S-Benzyl-L-cysteine
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|a Sulfur assimilation
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|a Cysteine
|2 NLM
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|a K848JZ4886
|2 NLM
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|a Cysteine Synthase
|2 NLM
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|a EC 2.5.1.47
|2 NLM
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| 650 |
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|a Herbicides
|2 NLM
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|a Lyases
|2 NLM
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|a EC 4.-
|2 NLM
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|a O-acetylserine
|2 NLM
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| 650 |
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|a G05L7T7ZEQ
|2 NLM
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| 650 |
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|a S-benzylcysteine
|2 NLM
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| 650 |
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|a 9VRE13M548
|2 NLM
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|a Sulfhydryl Compounds
|2 NLM
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| 700 |
1 |
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|a Abrahão, Josielle
|e verfasserin
|4 aut
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|a Siqueira-Soares, Rita de Cássia
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|a Contesoto, Isabela de Carvalho
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|a Grizza, Luiz Henryque Escher
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|a de Almeida, Guilherme Henrique Gonçalves
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|a Constantin, Renato Polimeni
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|a Philippsen, Gisele Strieder
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|a Seixas, Flavio Augusto Vicente
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|a Bueno, Paulo Sérgio Alves
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|a de Oliveira, Marco Aurélio Schüler
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|a Constantin, Rodrigo Polimeni
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|a Dos Santos, Wanderley Dantas
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|a Ferrarese-Filho, Osvaldo
|e verfasserin
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|a Marchiosi, Rogério
|e verfasserin
|4 aut
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| 773 |
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|i Enthalten in
|t Plant physiology and biochemistry : PPB
|d 1991
|g 204(2023) vom: 26. Nov., Seite 108127
|w (DE-627)NLM098178261
|x 1873-2690
|7 nnas
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| 773 |
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|g volume:204
|g year:2023
|g day:26
|g month:11
|g pages:108127
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|u http://dx.doi.org/10.1016/j.plaphy.2023.108127
|3 Volltext
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