Inhibition of O -acetylserine (thiol) lyase as a promising new mechanism of action for herbicides

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...
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Autor*in:	Foletto-Felipe, Marcela de Paiva [verfasserIn] Abrahão, Josielle [verfasserIn] Siqueira-Soares, Rita de Cássia [verfasserIn] Contesoto, Isabela de Carvalho [verfasserIn] Grizza, Luiz Henryque Escher [verfasserIn] de Almeida, Guilherme Henrique Gonçalves [verfasserIn] Constantin, Renato Polimeni [verfasserIn] Philippsen, Gisele Strieder [verfasserIn] Seixas, Flavio Augusto Vicente [verfasserIn] Bueno, Paulo Sérgio Alves [verfasserIn] de Oliveira, Marco Aurélio Schüler [verfasserIn] Constantin, Rodrigo Polimeni [verfasserIn] dos Santos, Wanderley Dantas [verfasserIn] Ferrarese-Filho, Osvaldo [verfasserIn] Marchiosi, Rogério [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2023

Schlagwörter:	Bioinformatics L-cysteine Sulfur assimilation New herbicidal action site

Übergeordnetes Werk:	Enthalten in: Plant physiology and biochemistry - Amsterdam [u.a.] : Elsevier Science, 1998, 204
Übergeordnetes Werk:	volume:204

DOI / URN:	10.1016/j.plaphy.2023.108127

Katalog-ID:	ELV065549260

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520			\|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 K ic of 4.29 mM and a K iu 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.
650		4	\|a Bioinformatics
650		4	\|a L-cysteine
650		4	\|a Sulfur assimilation
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700	1		\|a Abrahão, Josielle \|e verfasserin \|0 (orcid)0000-0003-3465-6895 \|4 aut
700	1		\|a Siqueira-Soares, Rita de Cássia \|e verfasserin \|4 aut
700	1		\|a Contesoto, Isabela de Carvalho \|e verfasserin \|4 aut
700	1		\|a Grizza, Luiz Henryque Escher \|e verfasserin \|0 (orcid)0000-0002-6587-4986 \|4 aut
700	1		\|a de Almeida, Guilherme Henrique Gonçalves \|e verfasserin \|4 aut
700	1		\|a Constantin, Renato Polimeni \|e verfasserin \|4 aut
700	1		\|a Philippsen, Gisele Strieder \|e verfasserin \|0 (orcid)0000-0002-4725-2323 \|4 aut
700	1		\|a Seixas, Flavio Augusto Vicente \|e verfasserin \|0 (orcid)0000-0002-0117-6919 \|4 aut
700	1		\|a Bueno, Paulo Sérgio Alves \|e verfasserin \|0 (orcid)0000-0002-6506-4668 \|4 aut
700	1		\|a de Oliveira, Marco Aurélio Schüler \|e verfasserin \|0 (orcid)0000-0002-1993-7771 \|4 aut
700	1		\|a Constantin, Rodrigo Polimeni \|e verfasserin \|4 aut
700	1		\|a dos Santos, Wanderley Dantas \|e verfasserin \|4 aut
700	1		\|a Ferrarese-Filho, Osvaldo \|e verfasserin \|0 (orcid)0000-0002-3477-4544 \|4 aut
700	1		\|a Marchiosi, Rogério \|e verfasserin \|0 (orcid)0000-0002-8386-2524 \|4 aut
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allfields	10.1016/j.plaphy.2023.108127 doi (DE-627)ELV065549260 (ELSEVIER)S0981-9428(23)00638-1 DE-627 ger DE-627 rda eng 630 640 580 VZ BIODIV DE-30 fid 42.00 bkl Foletto-Felipe, Marcela de Paiva verfasserin aut Inhibition of O -acetylserine (thiol) lyase as a promising new mechanism of action for herbicides 2023 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier 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 K ic of 4.29 mM and a K iu 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. Bioinformatics L-cysteine Sulfur assimilation New herbicidal action site Abrahão, Josielle verfasserin (orcid)0000-0003-3465-6895 aut Siqueira-Soares, Rita de Cássia verfasserin aut Contesoto, Isabela de Carvalho verfasserin aut Grizza, Luiz Henryque Escher verfasserin (orcid)0000-0002-6587-4986 aut de Almeida, Guilherme Henrique Gonçalves verfasserin aut Constantin, Renato Polimeni verfasserin aut Philippsen, Gisele Strieder verfasserin (orcid)0000-0002-4725-2323 aut Seixas, Flavio Augusto Vicente verfasserin (orcid)0000-0002-0117-6919 aut Bueno, Paulo Sérgio Alves verfasserin (orcid)0000-0002-6506-4668 aut de Oliveira, Marco Aurélio Schüler verfasserin (orcid)0000-0002-1993-7771 aut Constantin, Rodrigo Polimeni verfasserin aut dos Santos, Wanderley Dantas verfasserin aut Ferrarese-Filho, Osvaldo verfasserin (orcid)0000-0002-3477-4544 aut Marchiosi, Rogério verfasserin (orcid)0000-0002-8386-2524 aut Enthalten in Plant physiology and biochemistry Amsterdam [u.a.] : Elsevier Science, 1998 204 Online-Ressource (DE-627)324869193 (DE-600)2031431-0 (DE-576)094080925 1873-2690 nnns volume:204 GBV_USEFLAG_U GBV_ELV SYSFLAG_U FID-BIODIV GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_100 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2088 GBV_ILN_2106 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4242 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 42.00 Biologie: Allgemeines VZ AR 204
spelling	10.1016/j.plaphy.2023.108127 doi (DE-627)ELV065549260 (ELSEVIER)S0981-9428(23)00638-1 DE-627 ger DE-627 rda eng 630 640 580 VZ BIODIV DE-30 fid 42.00 bkl Foletto-Felipe, Marcela de Paiva verfasserin aut Inhibition of O -acetylserine (thiol) lyase as a promising new mechanism of action for herbicides 2023 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier 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 K ic of 4.29 mM and a K iu 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. Bioinformatics L-cysteine Sulfur assimilation New herbicidal action site Abrahão, Josielle verfasserin (orcid)0000-0003-3465-6895 aut Siqueira-Soares, Rita de Cássia verfasserin aut Contesoto, Isabela de Carvalho verfasserin aut Grizza, Luiz Henryque Escher verfasserin (orcid)0000-0002-6587-4986 aut de Almeida, Guilherme Henrique Gonçalves verfasserin aut Constantin, Renato Polimeni verfasserin aut Philippsen, Gisele Strieder verfasserin (orcid)0000-0002-4725-2323 aut Seixas, Flavio Augusto Vicente verfasserin (orcid)0000-0002-0117-6919 aut Bueno, Paulo Sérgio Alves verfasserin (orcid)0000-0002-6506-4668 aut de Oliveira, Marco Aurélio Schüler verfasserin (orcid)0000-0002-1993-7771 aut Constantin, Rodrigo Polimeni verfasserin aut dos Santos, Wanderley Dantas verfasserin aut Ferrarese-Filho, Osvaldo verfasserin (orcid)0000-0002-3477-4544 aut Marchiosi, Rogério verfasserin (orcid)0000-0002-8386-2524 aut Enthalten in Plant physiology and biochemistry Amsterdam [u.a.] : Elsevier Science, 1998 204 Online-Ressource (DE-627)324869193 (DE-600)2031431-0 (DE-576)094080925 1873-2690 nnns volume:204 GBV_USEFLAG_U GBV_ELV SYSFLAG_U FID-BIODIV GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_100 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2088 GBV_ILN_2106 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4242 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 42.00 Biologie: Allgemeines VZ AR 204
allfields_unstemmed	10.1016/j.plaphy.2023.108127 doi (DE-627)ELV065549260 (ELSEVIER)S0981-9428(23)00638-1 DE-627 ger DE-627 rda eng 630 640 580 VZ BIODIV DE-30 fid 42.00 bkl Foletto-Felipe, Marcela de Paiva verfasserin aut Inhibition of O -acetylserine (thiol) lyase as a promising new mechanism of action for herbicides 2023 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier 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 K ic of 4.29 mM and a K iu 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. Bioinformatics L-cysteine Sulfur assimilation New herbicidal action site Abrahão, Josielle verfasserin (orcid)0000-0003-3465-6895 aut Siqueira-Soares, Rita de Cássia verfasserin aut Contesoto, Isabela de Carvalho verfasserin aut Grizza, Luiz Henryque Escher verfasserin (orcid)0000-0002-6587-4986 aut de Almeida, Guilherme Henrique Gonçalves verfasserin aut Constantin, Renato Polimeni verfasserin aut Philippsen, Gisele Strieder verfasserin (orcid)0000-0002-4725-2323 aut Seixas, Flavio Augusto Vicente verfasserin (orcid)0000-0002-0117-6919 aut Bueno, Paulo Sérgio Alves verfasserin (orcid)0000-0002-6506-4668 aut de Oliveira, Marco Aurélio Schüler verfasserin (orcid)0000-0002-1993-7771 aut Constantin, Rodrigo Polimeni verfasserin aut dos Santos, Wanderley Dantas verfasserin aut Ferrarese-Filho, Osvaldo verfasserin (orcid)0000-0002-3477-4544 aut Marchiosi, Rogério verfasserin (orcid)0000-0002-8386-2524 aut Enthalten in Plant physiology and biochemistry Amsterdam [u.a.] : Elsevier Science, 1998 204 Online-Ressource (DE-627)324869193 (DE-600)2031431-0 (DE-576)094080925 1873-2690 nnns volume:204 GBV_USEFLAG_U GBV_ELV SYSFLAG_U FID-BIODIV GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_100 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2088 GBV_ILN_2106 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4242 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 42.00 Biologie: Allgemeines VZ AR 204
allfieldsGer	10.1016/j.plaphy.2023.108127 doi (DE-627)ELV065549260 (ELSEVIER)S0981-9428(23)00638-1 DE-627 ger DE-627 rda eng 630 640 580 VZ BIODIV DE-30 fid 42.00 bkl Foletto-Felipe, Marcela de Paiva verfasserin aut Inhibition of O -acetylserine (thiol) lyase as a promising new mechanism of action for herbicides 2023 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier 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 K ic of 4.29 mM and a K iu 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. Bioinformatics L-cysteine Sulfur assimilation New herbicidal action site Abrahão, Josielle verfasserin (orcid)0000-0003-3465-6895 aut Siqueira-Soares, Rita de Cássia verfasserin aut Contesoto, Isabela de Carvalho verfasserin aut Grizza, Luiz Henryque Escher verfasserin (orcid)0000-0002-6587-4986 aut de Almeida, Guilherme Henrique Gonçalves verfasserin aut Constantin, Renato Polimeni verfasserin aut Philippsen, Gisele Strieder verfasserin (orcid)0000-0002-4725-2323 aut Seixas, Flavio Augusto Vicente verfasserin (orcid)0000-0002-0117-6919 aut Bueno, Paulo Sérgio Alves verfasserin (orcid)0000-0002-6506-4668 aut de Oliveira, Marco Aurélio Schüler verfasserin (orcid)0000-0002-1993-7771 aut Constantin, Rodrigo Polimeni verfasserin aut dos Santos, Wanderley Dantas verfasserin aut Ferrarese-Filho, Osvaldo verfasserin (orcid)0000-0002-3477-4544 aut Marchiosi, Rogério verfasserin (orcid)0000-0002-8386-2524 aut Enthalten in Plant physiology and biochemistry Amsterdam [u.a.] : Elsevier Science, 1998 204 Online-Ressource (DE-627)324869193 (DE-600)2031431-0 (DE-576)094080925 1873-2690 nnns volume:204 GBV_USEFLAG_U GBV_ELV SYSFLAG_U FID-BIODIV GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_100 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2088 GBV_ILN_2106 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4242 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 42.00 Biologie: Allgemeines VZ AR 204
allfieldsSound	10.1016/j.plaphy.2023.108127 doi (DE-627)ELV065549260 (ELSEVIER)S0981-9428(23)00638-1 DE-627 ger DE-627 rda eng 630 640 580 VZ BIODIV DE-30 fid 42.00 bkl Foletto-Felipe, Marcela de Paiva verfasserin aut Inhibition of O -acetylserine (thiol) lyase as a promising new mechanism of action for herbicides 2023 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier 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 K ic of 4.29 mM and a K iu 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. Bioinformatics L-cysteine Sulfur assimilation New herbicidal action site Abrahão, Josielle verfasserin (orcid)0000-0003-3465-6895 aut Siqueira-Soares, Rita de Cássia verfasserin aut Contesoto, Isabela de Carvalho verfasserin aut Grizza, Luiz Henryque Escher verfasserin (orcid)0000-0002-6587-4986 aut de Almeida, Guilherme Henrique Gonçalves verfasserin aut Constantin, Renato Polimeni verfasserin aut Philippsen, Gisele Strieder verfasserin (orcid)0000-0002-4725-2323 aut Seixas, Flavio Augusto Vicente verfasserin (orcid)0000-0002-0117-6919 aut Bueno, Paulo Sérgio Alves verfasserin (orcid)0000-0002-6506-4668 aut de Oliveira, Marco Aurélio Schüler verfasserin (orcid)0000-0002-1993-7771 aut Constantin, Rodrigo Polimeni verfasserin aut dos Santos, Wanderley Dantas verfasserin aut Ferrarese-Filho, Osvaldo verfasserin (orcid)0000-0002-3477-4544 aut Marchiosi, Rogério verfasserin (orcid)0000-0002-8386-2524 aut Enthalten in Plant physiology and biochemistry Amsterdam [u.a.] : Elsevier Science, 1998 204 Online-Ressource (DE-627)324869193 (DE-600)2031431-0 (DE-576)094080925 1873-2690 nnns volume:204 GBV_USEFLAG_U GBV_ELV SYSFLAG_U FID-BIODIV GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_100 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2088 GBV_ILN_2106 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4242 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 42.00 Biologie: Allgemeines VZ AR 204
language	English
source	Enthalten in Plant physiology and biochemistry 204 volume:204
sourceStr	Enthalten in Plant physiology and biochemistry 204 volume:204
format_phy_str_mv	Article
bklname	Biologie: Allgemeines
institution	findex.gbv.de
topic_facet	Bioinformatics L-cysteine Sulfur assimilation New herbicidal action site
dewey-raw	630
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container_title	Plant physiology and biochemistry
authorswithroles_txt_mv	Foletto-Felipe, Marcela de Paiva @@aut@@ Abrahão, Josielle @@aut@@ Siqueira-Soares, Rita de Cássia @@aut@@ Contesoto, Isabela de Carvalho @@aut@@ Grizza, Luiz Henryque Escher @@aut@@ de Almeida, Guilherme Henrique Gonçalves @@aut@@ Constantin, Renato Polimeni @@aut@@ Philippsen, Gisele Strieder @@aut@@ Seixas, Flavio Augusto Vicente @@aut@@ Bueno, Paulo Sérgio Alves @@aut@@ de Oliveira, Marco Aurélio Schüler @@aut@@ Constantin, Rodrigo Polimeni @@aut@@ dos Santos, Wanderley Dantas @@aut@@ Ferrarese-Filho, Osvaldo @@aut@@ Marchiosi, Rogério @@aut@@
publishDateDaySort_date	2023-01-01T00:00:00Z
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author	Foletto-Felipe, Marcela de Paiva
spellingShingle	Foletto-Felipe, Marcela de Paiva ddc 630 fid BIODIV bkl 42.00 misc Bioinformatics misc L-cysteine misc Sulfur assimilation misc New herbicidal action site Inhibition of O -acetylserine (thiol) lyase as a promising new mechanism of action for herbicides
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title_full	Inhibition of O -acetylserine (thiol) lyase as a promising new mechanism of action for herbicides
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title_sort	inhibition of o -acetylserine (thiol) lyase as a promising new mechanism of action for herbicides
title_auth	Inhibition of O -acetylserine (thiol) lyase as a promising new mechanism of action for herbicides
abstract	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 K ic of 4.29 mM and a K iu 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.
abstractGer	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 K ic of 4.29 mM and a K iu 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.
abstract_unstemmed	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 K ic of 4.29 mM and a K iu 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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title_short	Inhibition of O -acetylserine (thiol) lyase as a promising new mechanism of action for herbicides
remote_bool	true
author2	Abrahão, Josielle Siqueira-Soares, Rita de Cássia Contesoto, Isabela de Carvalho Grizza, Luiz Henryque Escher de Almeida, Guilherme Henrique Gonçalves Constantin, Renato Polimeni Philippsen, Gisele Strieder Seixas, Flavio Augusto Vicente Bueno, Paulo Sérgio Alves de Oliveira, Marco Aurélio Schüler Constantin, Rodrigo Polimeni dos Santos, Wanderley Dantas Ferrarese-Filho, Osvaldo Marchiosi, Rogério
author2Str	Abrahão, Josielle Siqueira-Soares, Rita de Cássia Contesoto, Isabela de Carvalho Grizza, Luiz Henryque Escher de Almeida, Guilherme Henrique Gonçalves Constantin, Renato Polimeni Philippsen, Gisele Strieder Seixas, Flavio Augusto Vicente Bueno, Paulo Sérgio Alves de Oliveira, Marco Aurélio Schüler Constantin, Rodrigo Polimeni dos Santos, Wanderley Dantas Ferrarese-Filho, Osvaldo Marchiosi, Rogério
ppnlink	324869193
mediatype_str_mv	c
isOA_txt	false
hochschulschrift_bool	false
doi_str	10.1016/j.plaphy.2023.108127
up_date	2024-07-06T23:25:17.203Z
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