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psim  (Twist Bioscience)
86
Twist Bioscience psim
Comparison of absolute concentrations of indolethylamine products (median ± SD; n = 4 biological replicates; values are given in micrograms per gram per fresh weight) following transient expression of different combinations of AroG , PvTDC2 , and ( A ) PvNMT1 , PsiH , <t>PsiM</t> , and PsiK , or ( B ) OsCYP71P1 <t>,</t> <t>RmNMT</t> , AtCOMT , the mutant AtCOMTA160G , and PvNMT1 in N. benthamiana leaves. Absolute concentrations were according to external calibration curves. Concentrations of bufotenin 7 and 5-methoxy- N -methyltryptamine (5-MeO-NMT 9 ) were semiquantified using the calibration curves of psilocin 16 and 5-methoxy- N , N -dimethyltryptamine (5-MeO-DMT 10 ), respectively. Samples were collected 1 week following agroinfiltration. Unless otherwise stated, statistical significance was assessed using one-way ANOVA followed by Tukey’s post hoc test; different letters denote statistically significant differences ( P < 0.05). For psilocin 16 , 5-MeO-NMT 9 , and 5-MeO-DMT 10 , where ANOVA could not be applied due to zero variance in several gene combinations, statistical significance was assessed using two-tailed unpaired Student’s t test assuming unequal variance (** P < 0.01 and **** P < 0.0001; ns, not significant). Chemical structures of products are shown for reference and are colored according to . Additional pathway intermediates are shown in figs. S10 and S11. Plus signs indicate the biosynthetic genes included in each experiment; boxes mark the last enzyme added in a set of coexpressed genes. ( C ) AlphaFold3 model of AtCOMT bound to the cofactor SAM and substrate bufotenin 7 . Active sites of AtCOMT and the AtCOMTA160G variant are shown in insets I and II, respectively. Inset I: Steric overlap is observed between the residue of A160 (magenta) and the methyl groups of bufotenin 7 (purple spheres). Inset II: Substitution A160G (magenta, indicated by arrow) resolves the steric overlap, by removing the clashing methyl of A160, accommodating the bufotenin 7 methyl groups (purple spheres).
Psim, supplied by Twist Bioscience, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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psim  (Seqirus Inc)
86
Seqirus Inc psim
Comparison of absolute concentrations of indolethylamine products (median ± SD; n = 4 biological replicates; values are given in micrograms per gram per fresh weight) following transient expression of different combinations of AroG , PvTDC2 , and ( A ) PvNMT1 , PsiH , <t>PsiM</t> , and PsiK , or ( B ) OsCYP71P1 <t>,</t> <t>RmNMT</t> , AtCOMT , the mutant AtCOMTA160G , and PvNMT1 in N. benthamiana leaves. Absolute concentrations were according to external calibration curves. Concentrations of bufotenin 7 and 5-methoxy- N -methyltryptamine (5-MeO-NMT 9 ) were semiquantified using the calibration curves of psilocin 16 and 5-methoxy- N , N -dimethyltryptamine (5-MeO-DMT 10 ), respectively. Samples were collected 1 week following agroinfiltration. Unless otherwise stated, statistical significance was assessed using one-way ANOVA followed by Tukey’s post hoc test; different letters denote statistically significant differences ( P < 0.05). For psilocin 16 , 5-MeO-NMT 9 , and 5-MeO-DMT 10 , where ANOVA could not be applied due to zero variance in several gene combinations, statistical significance was assessed using two-tailed unpaired Student’s t test assuming unequal variance (** P < 0.01 and **** P < 0.0001; ns, not significant). Chemical structures of products are shown for reference and are colored according to . Additional pathway intermediates are shown in figs. S10 and S11. Plus signs indicate the biosynthetic genes included in each experiment; boxes mark the last enzyme added in a set of coexpressed genes. ( C ) AlphaFold3 model of AtCOMT bound to the cofactor SAM and substrate bufotenin 7 . Active sites of AtCOMT and the AtCOMTA160G variant are shown in insets I and II, respectively. Inset I: Steric overlap is observed between the residue of A160 (magenta) and the methyl groups of bufotenin 7 (purple spheres). Inset II: Substitution A160G (magenta, indicated by arrow) resolves the steric overlap, by removing the clashing methyl of A160, accommodating the bufotenin 7 methyl groups (purple spheres).
Psim, supplied by Seqirus Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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psim  (Powersim Inc)
90
Powersim Inc psim
Comparison of absolute concentrations of indolethylamine products (median ± SD; n = 4 biological replicates; values are given in micrograms per gram per fresh weight) following transient expression of different combinations of AroG , PvTDC2 , and ( A ) PvNMT1 , PsiH , <t>PsiM</t> , and PsiK , or ( B ) OsCYP71P1 <t>,</t> <t>RmNMT</t> , AtCOMT , the mutant AtCOMTA160G , and PvNMT1 in N. benthamiana leaves. Absolute concentrations were according to external calibration curves. Concentrations of bufotenin 7 and 5-methoxy- N -methyltryptamine (5-MeO-NMT 9 ) were semiquantified using the calibration curves of psilocin 16 and 5-methoxy- N , N -dimethyltryptamine (5-MeO-DMT 10 ), respectively. Samples were collected 1 week following agroinfiltration. Unless otherwise stated, statistical significance was assessed using one-way ANOVA followed by Tukey’s post hoc test; different letters denote statistically significant differences ( P < 0.05). For psilocin 16 , 5-MeO-NMT 9 , and 5-MeO-DMT 10 , where ANOVA could not be applied due to zero variance in several gene combinations, statistical significance was assessed using two-tailed unpaired Student’s t test assuming unequal variance (** P < 0.01 and **** P < 0.0001; ns, not significant). Chemical structures of products are shown for reference and are colored according to . Additional pathway intermediates are shown in figs. S10 and S11. Plus signs indicate the biosynthetic genes included in each experiment; boxes mark the last enzyme added in a set of coexpressed genes. ( C ) AlphaFold3 model of AtCOMT bound to the cofactor SAM and substrate bufotenin 7 . Active sites of AtCOMT and the AtCOMTA160G variant are shown in insets I and II, respectively. Inset I: Steric overlap is observed between the residue of A160 (magenta) and the methyl groups of bufotenin 7 (purple spheres). Inset II: Substitution A160G (magenta, indicated by arrow) resolves the steric overlap, by removing the clashing methyl of A160, accommodating the bufotenin 7 methyl groups (purple spheres).
Psim, supplied by Powersim Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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psim  (Verizon Communications)
90
Verizon Communications psim
Comparison of absolute concentrations of indolethylamine products (median ± SD; n = 4 biological replicates; values are given in micrograms per gram per fresh weight) following transient expression of different combinations of AroG , PvTDC2 , and ( A ) PvNMT1 , PsiH , <t>PsiM</t> , and PsiK , or ( B ) OsCYP71P1 <t>,</t> <t>RmNMT</t> , AtCOMT , the mutant AtCOMTA160G , and PvNMT1 in N. benthamiana leaves. Absolute concentrations were according to external calibration curves. Concentrations of bufotenin 7 and 5-methoxy- N -methyltryptamine (5-MeO-NMT 9 ) were semiquantified using the calibration curves of psilocin 16 and 5-methoxy- N , N -dimethyltryptamine (5-MeO-DMT 10 ), respectively. Samples were collected 1 week following agroinfiltration. Unless otherwise stated, statistical significance was assessed using one-way ANOVA followed by Tukey’s post hoc test; different letters denote statistically significant differences ( P < 0.05). For psilocin 16 , 5-MeO-NMT 9 , and 5-MeO-DMT 10 , where ANOVA could not be applied due to zero variance in several gene combinations, statistical significance was assessed using two-tailed unpaired Student’s t test assuming unequal variance (** P < 0.01 and **** P < 0.0001; ns, not significant). Chemical structures of products are shown for reference and are colored according to . Additional pathway intermediates are shown in figs. S10 and S11. Plus signs indicate the biosynthetic genes included in each experiment; boxes mark the last enzyme added in a set of coexpressed genes. ( C ) AlphaFold3 model of AtCOMT bound to the cofactor SAM and substrate bufotenin 7 . Active sites of AtCOMT and the AtCOMTA160G variant are shown in insets I and II, respectively. Inset I: Steric overlap is observed between the residue of A160 (magenta) and the methyl groups of bufotenin 7 (purple spheres). Inset II: Substitution A160G (magenta, indicated by arrow) resolves the steric overlap, by removing the clashing methyl of A160, accommodating the bufotenin 7 methyl groups (purple spheres).
Psim, supplied by Verizon Communications, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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psim 2022.3 software package  (Altair Engineering Inc)
90
Altair Engineering Inc psim 2022.3 software package
Comparison of absolute concentrations of indolethylamine products (median ± SD; n = 4 biological replicates; values are given in micrograms per gram per fresh weight) following transient expression of different combinations of AroG , PvTDC2 , and ( A ) PvNMT1 , PsiH , <t>PsiM</t> , and PsiK , or ( B ) OsCYP71P1 <t>,</t> <t>RmNMT</t> , AtCOMT , the mutant AtCOMTA160G , and PvNMT1 in N. benthamiana leaves. Absolute concentrations were according to external calibration curves. Concentrations of bufotenin 7 and 5-methoxy- N -methyltryptamine (5-MeO-NMT 9 ) were semiquantified using the calibration curves of psilocin 16 and 5-methoxy- N , N -dimethyltryptamine (5-MeO-DMT 10 ), respectively. Samples were collected 1 week following agroinfiltration. Unless otherwise stated, statistical significance was assessed using one-way ANOVA followed by Tukey’s post hoc test; different letters denote statistically significant differences ( P < 0.05). For psilocin 16 , 5-MeO-NMT 9 , and 5-MeO-DMT 10 , where ANOVA could not be applied due to zero variance in several gene combinations, statistical significance was assessed using two-tailed unpaired Student’s t test assuming unequal variance (** P < 0.01 and **** P < 0.0001; ns, not significant). Chemical structures of products are shown for reference and are colored according to . Additional pathway intermediates are shown in figs. S10 and S11. Plus signs indicate the biosynthetic genes included in each experiment; boxes mark the last enzyme added in a set of coexpressed genes. ( C ) AlphaFold3 model of AtCOMT bound to the cofactor SAM and substrate bufotenin 7 . Active sites of AtCOMT and the AtCOMTA160G variant are shown in insets I and II, respectively. Inset I: Steric overlap is observed between the residue of A160 (magenta) and the methyl groups of bufotenin 7 (purple spheres). Inset II: Substitution A160G (magenta, indicated by arrow) resolves the steric overlap, by removing the clashing methyl of A160, accommodating the bufotenin 7 methyl groups (purple spheres).
Psim 2022.3 Software Package, supplied by Altair Engineering Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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psim 2022.3 software package - by Bioz Stars, 2026-06
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psim software  (Powersim Inc)
90
Powersim Inc psim software
Comparison of absolute concentrations of indolethylamine products (median ± SD; n = 4 biological replicates; values are given in micrograms per gram per fresh weight) following transient expression of different combinations of AroG , PvTDC2 , and ( A ) PvNMT1 , PsiH , <t>PsiM</t> , and PsiK , or ( B ) OsCYP71P1 <t>,</t> <t>RmNMT</t> , AtCOMT , the mutant AtCOMTA160G , and PvNMT1 in N. benthamiana leaves. Absolute concentrations were according to external calibration curves. Concentrations of bufotenin 7 and 5-methoxy- N -methyltryptamine (5-MeO-NMT 9 ) were semiquantified using the calibration curves of psilocin 16 and 5-methoxy- N , N -dimethyltryptamine (5-MeO-DMT 10 ), respectively. Samples were collected 1 week following agroinfiltration. Unless otherwise stated, statistical significance was assessed using one-way ANOVA followed by Tukey’s post hoc test; different letters denote statistically significant differences ( P < 0.05). For psilocin 16 , 5-MeO-NMT 9 , and 5-MeO-DMT 10 , where ANOVA could not be applied due to zero variance in several gene combinations, statistical significance was assessed using two-tailed unpaired Student’s t test assuming unequal variance (** P < 0.01 and **** P < 0.0001; ns, not significant). Chemical structures of products are shown for reference and are colored according to . Additional pathway intermediates are shown in figs. S10 and S11. Plus signs indicate the biosynthetic genes included in each experiment; boxes mark the last enzyme added in a set of coexpressed genes. ( C ) AlphaFold3 model of AtCOMT bound to the cofactor SAM and substrate bufotenin 7 . Active sites of AtCOMT and the AtCOMTA160G variant are shown in insets I and II, respectively. Inset I: Steric overlap is observed between the residue of A160 (magenta) and the methyl groups of bufotenin 7 (purple spheres). Inset II: Substitution A160G (magenta, indicated by arrow) resolves the steric overlap, by removing the clashing methyl of A160, accommodating the bufotenin 7 methyl groups (purple spheres).
Psim Software, supplied by Powersim Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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psim software - by Bioz Stars, 2026-06
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psim-sah-(nor)baeocystin complexes  (Usona Institute Inc)
90
Usona Institute Inc psim-sah-(nor)baeocystin complexes
Comparison of absolute concentrations of indolethylamine products (median ± SD; n = 4 biological replicates; values are given in micrograms per gram per fresh weight) following transient expression of different combinations of AroG , PvTDC2 , and ( A ) PvNMT1 , PsiH , <t>PsiM</t> , and PsiK , or ( B ) OsCYP71P1 <t>,</t> <t>RmNMT</t> , AtCOMT , the mutant AtCOMTA160G , and PvNMT1 in N. benthamiana leaves. Absolute concentrations were according to external calibration curves. Concentrations of bufotenin 7 and 5-methoxy- N -methyltryptamine (5-MeO-NMT 9 ) were semiquantified using the calibration curves of psilocin 16 and 5-methoxy- N , N -dimethyltryptamine (5-MeO-DMT 10 ), respectively. Samples were collected 1 week following agroinfiltration. Unless otherwise stated, statistical significance was assessed using one-way ANOVA followed by Tukey’s post hoc test; different letters denote statistically significant differences ( P < 0.05). For psilocin 16 , 5-MeO-NMT 9 , and 5-MeO-DMT 10 , where ANOVA could not be applied due to zero variance in several gene combinations, statistical significance was assessed using two-tailed unpaired Student’s t test assuming unequal variance (** P < 0.01 and **** P < 0.0001; ns, not significant). Chemical structures of products are shown for reference and are colored according to . Additional pathway intermediates are shown in figs. S10 and S11. Plus signs indicate the biosynthetic genes included in each experiment; boxes mark the last enzyme added in a set of coexpressed genes. ( C ) AlphaFold3 model of AtCOMT bound to the cofactor SAM and substrate bufotenin 7 . Active sites of AtCOMT and the AtCOMTA160G variant are shown in insets I and II, respectively. Inset I: Steric overlap is observed between the residue of A160 (magenta) and the methyl groups of bufotenin 7 (purple spheres). Inset II: Substitution A160G (magenta, indicated by arrow) resolves the steric overlap, by removing the clashing methyl of A160, accommodating the bufotenin 7 methyl groups (purple spheres).
Psim Sah (Nor)baeocystin Complexes, supplied by Usona Institute Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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phosphatase inhibitor mixture psim  (Beyotime)
90
Beyotime phosphatase inhibitor mixture psim
Comparison of absolute concentrations of indolethylamine products (median ± SD; n = 4 biological replicates; values are given in micrograms per gram per fresh weight) following transient expression of different combinations of AroG , PvTDC2 , and ( A ) PvNMT1 , PsiH , <t>PsiM</t> , and PsiK , or ( B ) OsCYP71P1 <t>,</t> <t>RmNMT</t> , AtCOMT , the mutant AtCOMTA160G , and PvNMT1 in N. benthamiana leaves. Absolute concentrations were according to external calibration curves. Concentrations of bufotenin 7 and 5-methoxy- N -methyltryptamine (5-MeO-NMT 9 ) were semiquantified using the calibration curves of psilocin 16 and 5-methoxy- N , N -dimethyltryptamine (5-MeO-DMT 10 ), respectively. Samples were collected 1 week following agroinfiltration. Unless otherwise stated, statistical significance was assessed using one-way ANOVA followed by Tukey’s post hoc test; different letters denote statistically significant differences ( P < 0.05). For psilocin 16 , 5-MeO-NMT 9 , and 5-MeO-DMT 10 , where ANOVA could not be applied due to zero variance in several gene combinations, statistical significance was assessed using two-tailed unpaired Student’s t test assuming unequal variance (** P < 0.01 and **** P < 0.0001; ns, not significant). Chemical structures of products are shown for reference and are colored according to . Additional pathway intermediates are shown in figs. S10 and S11. Plus signs indicate the biosynthetic genes included in each experiment; boxes mark the last enzyme added in a set of coexpressed genes. ( C ) AlphaFold3 model of AtCOMT bound to the cofactor SAM and substrate bufotenin 7 . Active sites of AtCOMT and the AtCOMTA160G variant are shown in insets I and II, respectively. Inset I: Steric overlap is observed between the residue of A160 (magenta) and the methyl groups of bufotenin 7 (purple spheres). Inset II: Substitution A160G (magenta, indicated by arrow) resolves the steric overlap, by removing the clashing methyl of A160, accommodating the bufotenin 7 methyl groups (purple spheres).
Phosphatase Inhibitor Mixture Psim, supplied by Beyotime, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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psim module  (ASPEC Technologies Limited)
90
ASPEC Technologies Limited psim module
Comparison of absolute concentrations of indolethylamine products (median ± SD; n = 4 biological replicates; values are given in micrograms per gram per fresh weight) following transient expression of different combinations of AroG , PvTDC2 , and ( A ) PvNMT1 , PsiH , <t>PsiM</t> , and PsiK , or ( B ) OsCYP71P1 <t>,</t> <t>RmNMT</t> , AtCOMT , the mutant AtCOMTA160G , and PvNMT1 in N. benthamiana leaves. Absolute concentrations were according to external calibration curves. Concentrations of bufotenin 7 and 5-methoxy- N -methyltryptamine (5-MeO-NMT 9 ) were semiquantified using the calibration curves of psilocin 16 and 5-methoxy- N , N -dimethyltryptamine (5-MeO-DMT 10 ), respectively. Samples were collected 1 week following agroinfiltration. Unless otherwise stated, statistical significance was assessed using one-way ANOVA followed by Tukey’s post hoc test; different letters denote statistically significant differences ( P < 0.05). For psilocin 16 , 5-MeO-NMT 9 , and 5-MeO-DMT 10 , where ANOVA could not be applied due to zero variance in several gene combinations, statistical significance was assessed using two-tailed unpaired Student’s t test assuming unequal variance (** P < 0.01 and **** P < 0.0001; ns, not significant). Chemical structures of products are shown for reference and are colored according to . Additional pathway intermediates are shown in figs. S10 and S11. Plus signs indicate the biosynthetic genes included in each experiment; boxes mark the last enzyme added in a set of coexpressed genes. ( C ) AlphaFold3 model of AtCOMT bound to the cofactor SAM and substrate bufotenin 7 . Active sites of AtCOMT and the AtCOMTA160G variant are shown in insets I and II, respectively. Inset I: Steric overlap is observed between the residue of A160 (magenta) and the methyl groups of bufotenin 7 (purple spheres). Inset II: Substitution A160G (magenta, indicated by arrow) resolves the steric overlap, by removing the clashing methyl of A160, accommodating the bufotenin 7 methyl groups (purple spheres).
Psim Module, supplied by ASPEC Technologies Limited, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Comparison of absolute concentrations of indolethylamine products (median ± SD; n = 4 biological replicates; values are given in micrograms per gram per fresh weight) following transient expression of different combinations of AroG , PvTDC2 , and ( A ) PvNMT1 , PsiH , PsiM , and PsiK , or ( B ) OsCYP71P1 , RmNMT , AtCOMT , the mutant AtCOMTA160G , and PvNMT1 in N. benthamiana leaves. Absolute concentrations were according to external calibration curves. Concentrations of bufotenin 7 and 5-methoxy- N -methyltryptamine (5-MeO-NMT 9 ) were semiquantified using the calibration curves of psilocin 16 and 5-methoxy- N , N -dimethyltryptamine (5-MeO-DMT 10 ), respectively. Samples were collected 1 week following agroinfiltration. Unless otherwise stated, statistical significance was assessed using one-way ANOVA followed by Tukey’s post hoc test; different letters denote statistically significant differences ( P < 0.05). For psilocin 16 , 5-MeO-NMT 9 , and 5-MeO-DMT 10 , where ANOVA could not be applied due to zero variance in several gene combinations, statistical significance was assessed using two-tailed unpaired Student’s t test assuming unequal variance (** P < 0.01 and **** P < 0.0001; ns, not significant). Chemical structures of products are shown for reference and are colored according to . Additional pathway intermediates are shown in figs. S10 and S11. Plus signs indicate the biosynthetic genes included in each experiment; boxes mark the last enzyme added in a set of coexpressed genes. ( C ) AlphaFold3 model of AtCOMT bound to the cofactor SAM and substrate bufotenin 7 . Active sites of AtCOMT and the AtCOMTA160G variant are shown in insets I and II, respectively. Inset I: Steric overlap is observed between the residue of A160 (magenta) and the methyl groups of bufotenin 7 (purple spheres). Inset II: Substitution A160G (magenta, indicated by arrow) resolves the steric overlap, by removing the clashing methyl of A160, accommodating the bufotenin 7 methyl groups (purple spheres).

Journal: Science Advances

Article Title: Complete biosynthesis of psychedelic tryptamines from three kingdoms in plants

doi: 10.1126/sciadv.aeb3034

Figure Lengend Snippet: Comparison of absolute concentrations of indolethylamine products (median ± SD; n = 4 biological replicates; values are given in micrograms per gram per fresh weight) following transient expression of different combinations of AroG , PvTDC2 , and ( A ) PvNMT1 , PsiH , PsiM , and PsiK , or ( B ) OsCYP71P1 , RmNMT , AtCOMT , the mutant AtCOMTA160G , and PvNMT1 in N. benthamiana leaves. Absolute concentrations were according to external calibration curves. Concentrations of bufotenin 7 and 5-methoxy- N -methyltryptamine (5-MeO-NMT 9 ) were semiquantified using the calibration curves of psilocin 16 and 5-methoxy- N , N -dimethyltryptamine (5-MeO-DMT 10 ), respectively. Samples were collected 1 week following agroinfiltration. Unless otherwise stated, statistical significance was assessed using one-way ANOVA followed by Tukey’s post hoc test; different letters denote statistically significant differences ( P < 0.05). For psilocin 16 , 5-MeO-NMT 9 , and 5-MeO-DMT 10 , where ANOVA could not be applied due to zero variance in several gene combinations, statistical significance was assessed using two-tailed unpaired Student’s t test assuming unequal variance (** P < 0.01 and **** P < 0.0001; ns, not significant). Chemical structures of products are shown for reference and are colored according to . Additional pathway intermediates are shown in figs. S10 and S11. Plus signs indicate the biosynthetic genes included in each experiment; boxes mark the last enzyme added in a set of coexpressed genes. ( C ) AlphaFold3 model of AtCOMT bound to the cofactor SAM and substrate bufotenin 7 . Active sites of AtCOMT and the AtCOMTA160G variant are shown in insets I and II, respectively. Inset I: Steric overlap is observed between the residue of A160 (magenta) and the methyl groups of bufotenin 7 (purple spheres). Inset II: Substitution A160G (magenta, indicated by arrow) resolves the steric overlap, by removing the clashing methyl of A160, accommodating the bufotenin 7 methyl groups (purple spheres).

Article Snippet: RmNMT , PsiH , PsiK , PsiM , OsCYP71P1 , AtCOMT , AtCOMTA160G , RebF , RebH , PyrH , and SttH coding sequences were codon optimized for expression in N. tabacum and synthesized by Twist Biosciences.

Techniques: Comparison, Expressing, Mutagenesis, Two Tailed Test, Variant Assay, Residue