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S-adenosyl-L-methionine + 3-hydroxybenzoate
methyl 3-hydroxybenzoate + S-adenosyl-L-homocysteine
26% activity compared to salicylate
-
-
?
S-adenosyl-L-methionine + 3-hydroxybenzoate
S-adenosyl-L-homocysteine + methyl 3-hydroxybenzoate
-
1.8% activity compared to salicylate
-
-
?
S-adenosyl-L-methionine + 3-hydroxybenzoic acid
S-adenosyl-L-homocysteine + methyl 3-hydroxybenzoate
S-adenosyl-L-methionine + 4-aminosalicylate
S-adenosyl-L-homocysteine + methyl 4-aminosalicylate
-
2% activity compared to salicylate
-
-
?
S-adenosyl-L-methionine + 4-hydroxybenzoate
S-adenosyl-L-homocysteine + methyl 4-hydroxybenzoate
-
lower catalytic efficiency with 4-hydroxybenzoate compared to salicylate
-
-
?
S-adenosyl-L-methionine + anthranilate
?
-
9.3% activity compared to salicylate
-
-
?
S-adenosyl-L-methionine + anthranilate
methyl anthranilate + S-adenosyl-L-homocysteine
-
-
-
?
S-adenosyl-L-methionine + anthranilic acid
S-adenosyl-L-homocysteine + methyl anthranilate
S-adenosyl-L-methionine + benzoate
?
-
16.9% activity compared to salicylate
-
-
?
S-adenosyl-L-methionine + benzoate
methyl benzoate + S-adenosyl-L-homocysteine
S-adenosyl-L-methionine + benzoate
S-adenosyl-L-homocysteine + methyl benzoate
-
2% activity compared to salicylate
-
-
?
S-adenosyl-L-methionine + cinnamic acid
S-adenosyl-L-homocysteine + methyl cinnamate
less than 2% relative activity at 1 mM methyl acceptor compared to activity with salicylate set at 100%
-
-
?
S-adenosyl-L-methionine + jasmonic acid
S-adenosyl-L-homocysteine + methyl jasmonate
Y147S/M150H double mutant and Y147S/M150H/F347Y triple mutant are able to turn over jasmonic acid, while preserving substantial salicylate methylating activity
-
-
?
S-adenosyl-L-methionine + salicylate
methyl salicylate + S-adenosyl-L-homocysteine
S-adenosyl-L-methionine + salicylate
S-adenosyl-L-homocysteine + methyl salicylate
S-adenosyl-L-methionine + salicylic acid
S-adenosyl-L-homocysteine + methyl salicylate
S-adenosyl-L-methionine + vanillate
methyl vanillate + S-adenosyl-L-homocysteine
12% activity compared to salicylate
-
-
?
S-adenosyl-L-methionine + vanillic acid
S-adenosyl-L-homocysteine + methyl 4-hydroxy-3-methoxybenzoate
5.1% activity of wild-type enzyme compared to salicylate methylation
-
-
?
additional information
?
-
S-adenosyl-L-methionine + 3-hydroxybenzoic acid
S-adenosyl-L-homocysteine + methyl 3-hydroxybenzoate
54% relative activity at 1 mM methyl acceptor compared to activity with benzoic acid set at 100%
-
-
?
S-adenosyl-L-methionine + 3-hydroxybenzoic acid
S-adenosyl-L-homocysteine + methyl 3-hydroxybenzoate
less than 2% relative activity at 1 mM methyl acceptor compared to activity with salicylate set at 100%
-
-
?
S-adenosyl-L-methionine + 3-hydroxybenzoic acid
S-adenosyl-L-homocysteine + methyl 3-hydroxybenzoate
17% activity of wild-type enzyme compared to salicylate methylation
-
-
?
S-adenosyl-L-methionine + anthranilic acid
S-adenosyl-L-homocysteine + methyl anthranilate
32% relative activity at 1 mM methyl acceptor compared to activity with benzoic acid set at 100%
-
-
?
S-adenosyl-L-methionine + anthranilic acid
S-adenosyl-L-homocysteine + methyl anthranilate
35% relative activity at 1 mM methyl acceptor compared to activity with benzoic acid set at 100%
-
-
?
S-adenosyl-L-methionine + benzoate
methyl benzoate + S-adenosyl-L-homocysteine
-
-
-
?
S-adenosyl-L-methionine + benzoate
methyl benzoate + S-adenosyl-L-homocysteine
-
-
-
?
S-adenosyl-L-methionine + benzoate
methyl benzoate + S-adenosyl-L-homocysteine
-
-
-
-
?
S-adenosyl-L-methionine + benzoate
methyl benzoate + S-adenosyl-L-homocysteine
96% activity compared to salicylate
-
-
?
S-adenosyl-L-methionine + benzoate
methyl benzoate + S-adenosyl-L-homocysteine
-
-
-
-
?
S-adenosyl-L-methionine + benzoate
methyl benzoate + S-adenosyl-L-homocysteine
-
8% activity compared to salicylate
-
-
?
S-adenosyl-L-methionine + benzoate
methyl benzoate + S-adenosyl-L-homocysteine
-
-
-
?
S-adenosyl-L-methionine + benzoate
methyl benzoate + S-adenosyl-L-homocysteine
-
-
-
?
S-adenosyl-L-methionine + salicylate
methyl salicylate + S-adenosyl-L-homocysteine
-
-
-
?
S-adenosyl-L-methionine + salicylate
methyl salicylate + S-adenosyl-L-homocysteine
-
-
-
?
S-adenosyl-L-methionine + salicylate
methyl salicylate + S-adenosyl-L-homocysteine
-
-
-
-
?
S-adenosyl-L-methionine + salicylate
methyl salicylate + S-adenosyl-L-homocysteine
-
-
-
?
S-adenosyl-L-methionine + salicylate
methyl salicylate + S-adenosyl-L-homocysteine
-
-
-
?
S-adenosyl-L-methionine + salicylate
methyl salicylate + S-adenosyl-L-homocysteine
best substrate
-
-
?
S-adenosyl-L-methionine + salicylate
methyl salicylate + S-adenosyl-L-homocysteine
-
-
-
?
S-adenosyl-L-methionine + salicylate
methyl salicylate + S-adenosyl-L-homocysteine
-
-
-
?
S-adenosyl-L-methionine + salicylate
methyl salicylate + S-adenosyl-L-homocysteine
-
-
-
-
?
S-adenosyl-L-methionine + salicylate
methyl salicylate + S-adenosyl-L-homocysteine
-
best substrate
-
-
?
S-adenosyl-L-methionine + salicylate
methyl salicylate + S-adenosyl-L-homocysteine
-
-
-
?
S-adenosyl-L-methionine + salicylate
methyl salicylate + S-adenosyl-L-homocysteine
-
-
-
?
S-adenosyl-L-methionine + salicylate
S-adenosyl-L-homocysteine + methyl salicylate
-
-
-
-
?
S-adenosyl-L-methionine + salicylate
S-adenosyl-L-homocysteine + methyl salicylate
-
-
-
-
?
S-adenosyl-L-methionine + salicylate
S-adenosyl-L-homocysteine + methyl salicylate
-
-
-
?
S-adenosyl-L-methionine + salicylate
S-adenosyl-L-homocysteine + methyl salicylate
-
-
-
-
?
S-adenosyl-L-methionine + salicylate
S-adenosyl-L-homocysteine + methyl salicylate
-
highest level of specific activity with salicylate
-
-
?
S-adenosyl-L-methionine + salicylate
S-adenosyl-L-homocysteine + methyl salicylate
-
-
-
?
S-adenosyl-L-methionine + salicylate
S-adenosyl-L-homocysteine + methyl salicylate
-
-
-
-
?
S-adenosyl-L-methionine + salicylate
S-adenosyl-L-homocysteine + methyl salicylate
-
-
-
?
S-adenosyl-L-methionine + salicylate
S-adenosyl-L-homocysteine + methyl salicylate
-
-
-
?
S-adenosyl-L-methionine + salicylate
S-adenosyl-L-homocysteine + methyl salicylate
-
100% activity
-
-
?
S-adenosyl-L-methionine + salicylic acid
S-adenosyl-L-homocysteine + methyl salicylate
-
-
-
?
S-adenosyl-L-methionine + salicylic acid
S-adenosyl-L-homocysteine + methyl salicylate
16% relative activity at 1 mM methyl acceptor compared to activity with benzoic acid set at 100%
-
-
?
S-adenosyl-L-methionine + salicylic acid
S-adenosyl-L-homocysteine + methyl salicylate
46% relative activity at 1 mM methyl acceptor compared to activity with benzoic acid set at 100%
-
-
?
additional information
?
-
enzyme is also active with benzoic acid resulting in methyl benzoate formation
-
-
?
additional information
?
-
-
enzyme is also active with benzoic acid resulting in methyl benzoate formation
-
-
?
additional information
?
-
no activity with 3-hydroxybenzoic acid, 4-hydroxybenzoic acid, trans-cinnamic acid, p-coumaric acid, m-coumaric acid, o-coumaric acid and benzyl alcohol
-
-
?
additional information
?
-
-
no activity with 3-hydroxybenzoic acid, 4-hydroxybenzoic acid, trans-cinnamic acid, p-coumaric acid, m-coumaric acid, o-coumaric acid and benzyl alcohol
-
-
?
additional information
?
-
enzyme is also active with benzoic acid resulting in methyl benzoate formation
-
-
?
additional information
?
-
in contrast to AtBSMT1 no activity with 1 mM 3-hydroxybenzoic acid
-
-
?
additional information
?
-
The enzyme, which is found in flowering plants, also has the activity of EC 2.1.1.273, benzoate O-methyltransferase
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-
?
additional information
?
-
enzyme is also active with benzoic acid resulting in methyl benzoate formation
-
-
?
additional information
?
-
The enzyme, which is found in flowering plants, also has the activity of EC 2.1.1.273, benzoate O-methyltransferase
-
-
?
additional information
?
-
substrate specificity of recombinant enzyme, overview
-
-
-
additional information
?
-
-
substrate specificity of recombinant enzyme, overview
-
-
-
additional information
?
-
enzyme is also active with benzoic acid resulting in methyl benzoate formation
-
-
?
additional information
?
-
no activity with 4-hydroxybenzoic acid, vanillic acid, caffeic acid, p-coumaric acid and (+/-)jasmonic acid
-
-
?
additional information
?
-
no measurable methylation of jasmonic acid by wild-type SAMT using concentrations up to 5 mM
-
-
?
additional information
?
-
-
no measurable methylation of jasmonic acid by wild-type SAMT using concentrations up to 5 mM
-
-
?
additional information
?
-
wild-type is also able to methylate benzoic acid with 48% activity compared to salicylate methylation
-
-
?
additional information
?
-
-
wild-type is also able to methylate benzoic acid with 48% activity compared to salicylate methylation
-
-
?
additional information
?
-
development and evaluation of an enzyme-coupled assay for monitoring methyltransferase activity, overview. Since S-adenosyl-L-homocysteine is a key by-product of reactions catalyzed by S-adenosyl methionine-dependent methyltransferases, the coupling enzymes are used to assess the activities of EcoRI methyltransferase and a salicylic acid methyltransferase from Clarkia breweri in the presence of S-adenosyl methionine. In the case of the salicylic acid methyltransferase, detectable activity is observed for several substrates including salicylic acid, benzoic acid, 3-hydroxybenzoic acid, and vanillic acid, substrate specificity, overview. Additionally, the de novo synthesis of the relatively expensive and unstable cosubstrate, S-adenosyl methionine, catalyzed by methionine adenosyltransferase can be incorporated within the assay. The assay offers a high level of sensitivity that permits continuous and reliable monitoring of methyltransferase activities. The assay enzymes, 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase (Mtn), xanthine oxidase (XOD), and horse radish peroxidase (HRP), are able to operate in a tandem manner to generate a fluorescence signal in the presence of SAH, the key by-product of reactions catalyzed by SAM-dependent methyltransferases. Poor or no substrates are acetate, propanoate, butyrate, 4-hydroxybenzoate, jasmonate, cinnamate, coumarate, and caffeate
-
-
-
additional information
?
-
-
jasmonic acid, indole-3-acetic acid and gibberellic acid do not serve as substrates for isoform SAMT1
-
-
?
additional information
?
-
GC-MS product identification
-
-
-
additional information
?
-
-
GC-MS product identification
-
-
-
additional information
?
-
the enzyme also catalyzes the reaction of benzoic acid carboxyl methyltransferase, EC 2.1.1.273
-
-
?
additional information
?
-
-
isozyme PaSABATH2 has the highest level of specific activity with salicylic acid and is designated as PaSAMT (EC 2.1.1.274). For comparison, PaSAMT is also assayed with two compounds of similar structure benzoic acid and anthranilic acid (cf. EC 2.1.1.273). While PaSAMT has no activity with anthranilic acid, its activity with benzoic acid is approximately 8% of that with salicylic acid. Radiochemical assay method
-
-
-
additional information
?
-
the enzyme also catalyzes the reaction of benzoic acid carboxyl methyltransferase, EC 2.1.1.273
-
-
?
additional information
?
-
-
the enzyme also catalyzes the reaction of benzoic acid carboxyl methyltransferase, EC 2.1.1.273
-
-
?
additional information
?
-
enzyme PtSABATH4 exhibits high enzymatic activity towards the substrate salicylate (SA) and weak activity towards benzoic acid, jasmonic acid, and farnesoic acid. PtSABATH4 does not show any activity towards indole-3-acetic acid, vanillic acid, nicotinic acid, coumalic acid, and trans-cinnamic acid. PtSABATH4 shows at least 4.3fold higher enzymatic activity towards the substrate SA. PtSABATH4 displays the highest level of catalytic activity towards SA and a relatively low level of activity towards BA. Preference for salicylic acid (SA) over benzoic acid (BA) in wild-type PtSABATH4 and preference for BA over SA in the PtSABATH4 M156H mutant
-
-
-
additional information
?
-
-
enzyme PtSABATH4 exhibits high enzymatic activity towards the substrate salicylate (SA) and weak activity towards benzoic acid, jasmonic acid, and farnesoic acid. PtSABATH4 does not show any activity towards indole-3-acetic acid, vanillic acid, nicotinic acid, coumalic acid, and trans-cinnamic acid. PtSABATH4 shows at least 4.3fold higher enzymatic activity towards the substrate SA. PtSABATH4 displays the highest level of catalytic activity towards SA and a relatively low level of activity towards BA. Preference for salicylic acid (SA) over benzoic acid (BA) in wild-type PtSABATH4 and preference for BA over SA in the PtSABATH4 M156H mutant
-
-
-
additional information
?
-
-
less than 1% activity with jasmonic acid, indole-3-acetic acid and gibberellic acid 3
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
S-adenosyl-L-methionine + 3-hydroxybenzoate
S-adenosyl-L-homocysteine + methyl 3-hydroxybenzoate
-
1.8% activity compared to salicylate
-
-
?
S-adenosyl-L-methionine + 4-aminosalicylate
S-adenosyl-L-homocysteine + methyl 4-aminosalicylate
-
2% activity compared to salicylate
-
-
?
S-adenosyl-L-methionine + 4-hydroxybenzoate
S-adenosyl-L-homocysteine + methyl 4-hydroxybenzoate
-
lower catalytic efficiency with 4-hydroxybenzoate compared to salicylate
-
-
?
S-adenosyl-L-methionine + anthranilate
?
-
9.3% activity compared to salicylate
-
-
?
S-adenosyl-L-methionine + benzoate
?
-
16.9% activity compared to salicylate
-
-
?
S-adenosyl-L-methionine + benzoate
methyl benzoate + S-adenosyl-L-homocysteine
S-adenosyl-L-methionine + benzoate
S-adenosyl-L-homocysteine + methyl benzoate
-
2% activity compared to salicylate
-
-
?
S-adenosyl-L-methionine + salicylate
methyl salicylate + S-adenosyl-L-homocysteine
S-adenosyl-L-methionine + salicylate
S-adenosyl-L-homocysteine + methyl salicylate
additional information
?
-
S-adenosyl-L-methionine + benzoate
methyl benzoate + S-adenosyl-L-homocysteine
-
-
-
?
S-adenosyl-L-methionine + benzoate
methyl benzoate + S-adenosyl-L-homocysteine
-
-
-
?
S-adenosyl-L-methionine + benzoate
methyl benzoate + S-adenosyl-L-homocysteine
-
-
-
-
?
S-adenosyl-L-methionine + benzoate
methyl benzoate + S-adenosyl-L-homocysteine
-
-
-
-
?
S-adenosyl-L-methionine + benzoate
methyl benzoate + S-adenosyl-L-homocysteine
-
-
-
?
S-adenosyl-L-methionine + benzoate
methyl benzoate + S-adenosyl-L-homocysteine
-
-
-
?
S-adenosyl-L-methionine + salicylate
methyl salicylate + S-adenosyl-L-homocysteine
-
-
-
?
S-adenosyl-L-methionine + salicylate
methyl salicylate + S-adenosyl-L-homocysteine
-
-
-
?
S-adenosyl-L-methionine + salicylate
methyl salicylate + S-adenosyl-L-homocysteine
-
-
-
-
?
S-adenosyl-L-methionine + salicylate
methyl salicylate + S-adenosyl-L-homocysteine
-
-
-
?
S-adenosyl-L-methionine + salicylate
methyl salicylate + S-adenosyl-L-homocysteine
-
-
-
?
S-adenosyl-L-methionine + salicylate
methyl salicylate + S-adenosyl-L-homocysteine
-
-
-
?
S-adenosyl-L-methionine + salicylate
methyl salicylate + S-adenosyl-L-homocysteine
-
-
-
?
S-adenosyl-L-methionine + salicylate
methyl salicylate + S-adenosyl-L-homocysteine
-
-
-
-
?
S-adenosyl-L-methionine + salicylate
methyl salicylate + S-adenosyl-L-homocysteine
-
-
-
?
S-adenosyl-L-methionine + salicylate
methyl salicylate + S-adenosyl-L-homocysteine
-
-
-
?
S-adenosyl-L-methionine + salicylate
S-adenosyl-L-homocysteine + methyl salicylate
-
-
-
-
?
S-adenosyl-L-methionine + salicylate
S-adenosyl-L-homocysteine + methyl salicylate
-
-
-
-
?
S-adenosyl-L-methionine + salicylate
S-adenosyl-L-homocysteine + methyl salicylate
-
-
-
?
S-adenosyl-L-methionine + salicylate
S-adenosyl-L-homocysteine + methyl salicylate
-
highest level of specific activity with salicylate
-
-
?
S-adenosyl-L-methionine + salicylate
S-adenosyl-L-homocysteine + methyl salicylate
-
-
-
?
S-adenosyl-L-methionine + salicylate
S-adenosyl-L-homocysteine + methyl salicylate
-
-
-
-
?
S-adenosyl-L-methionine + salicylate
S-adenosyl-L-homocysteine + methyl salicylate
-
-
-
?
S-adenosyl-L-methionine + salicylate
S-adenosyl-L-homocysteine + methyl salicylate
-
-
-
?
S-adenosyl-L-methionine + salicylate
S-adenosyl-L-homocysteine + methyl salicylate
-
100% activity
-
-
?
additional information
?
-
-
jasmonic acid, indole-3-acetic acid and gibberellic acid do not serve as substrates for isoform SAMT1
-
-
?
additional information
?
-
the enzyme also catalyzes the reaction of benzoic acid carboxyl methyltransferase, EC 2.1.1.273
-
-
?
additional information
?
-
the enzyme also catalyzes the reaction of benzoic acid carboxyl methyltransferase, EC 2.1.1.273
-
-
?
additional information
?
-
-
the enzyme also catalyzes the reaction of benzoic acid carboxyl methyltransferase, EC 2.1.1.273
-
-
?
additional information
?
-
-
less than 1% activity with jasmonic acid, indole-3-acetic acid and gibberellic acid 3
-
-
?
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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evolution
the enzyme belongs to SABATH family, a class of O-methyltransferases and N-methyltransferases
evolution
-
the enzyme belongs to the protein family of SABATH methyltransferases, ten genes encode isozymes PaSABATH1-10. Five of the PaSABATH isozymes (PaSABATH3, PaSABATH6, PaSABATH7, PaSABATH8, and PaSABATH9) do not show activity with any of the four substrates, i.e. indole-3-acetic acid, jasmonic acid, giberellic acid A3, and salicylic acid, the other five of the PaSABATHs each show activity with one or more of the four substrates. PaSABATH1 has the highest level of specific activity with indole-3-acetic acid and is renamed as PaIAMT (EC 2.1.1.275). PaSABATH2 has the highest level of specific activity with salicylic acid and is designated as PaSAMT (EC 2.1.1.274). For comparison, PaSAMT is also assayed with two compounds of similar structure benzoic acid and anthranilic acid (cf. EC 2.1.1.273). While PaSAMT has no activity with anthranilic acid, its activity with benzoic acid is approximately 8% of that with salicylic acid. PaSABATH4, PaSABATH5 and PaSABATH10 show the highest level of specific activity with jasmonic acid and are renamed PaJAMT1, PaJAMT2, and PaJAMT3, respectively (EC 2.1.1.141). Their products are confirmed to be methyljasmonate
evolution
the enzyme belongs to the SABATH family, phylogenetic analysis and tree, detailed overview. Twenty-eight Populus SABATH genes are divided into three classes with distinct divergences in their gene structure, expression responses to abiotic stressors and enzymatic properties of encoded proteins. Populus class I SABATH proteins convert indole-3-acetic acid (IAA) to methyl-IAA, class II SABATH proteins convert benzoic acid (BA) and salicylic acid (SA) to methyl-BA and methyl-SA, while class III SABATH proteins convert farnesoic acid (FA) to methyl-FA. For Populus class II SABATH proteins, both forward and reverse mutagenesis studies show that a single amino acid switch between PtSABATH4 and PtSABATH24 results in substrate switch. Of the Populus SABATH class II proteins, PtSABATH4 and 24 show the highest activity towards SA and BA, respectively
malfunction
-
a knockout mutant fails to accumulate methyl salicylate following pathogen infection. These plants also fail to accumulate salicylate or its glucoside in the uninoculated leaves and do not develop systemic acquired resistance. However, the mutant exhibits normal levels of effector-triggered immunity and pathogen-associated molecular pattern-triggered immunity to Pseudomonas syringae and Hyaloperonospora arabidopsidis
malfunction
AtBSMT1-overexpressing plants are not more susceptible than wild-type to either Plasmodiophora brassicae or Albugo candida. Transgenic Arabidopsis thaliana and Nicotiana tabacum plants overexpressing PbBSMT exhibit increased susceptibility to virulent Pseudomonas syringae pv. tomato DC3000 and virulent Pseudomonas syringae pv. tabaci, respectively. Gene-mediated resistance to DC3000/AvrRpt2 and tobacco mosaic virus (TMV) is also compromised in Arabidopsis thaliana and Nicotiana tabacum cv. Xanthi-nc plants overexpressing PbBSMT, respectively. Transient expression of PbBSMT or AtBSMT1 in lower leaves of Nicotiana tabacum Xanthi-nc results in systemic acquired resistance (SAR)-like enhanced resistance to TMV in the distal systemic leaves. The development of a PbBSMT-mediated SAR-like phenotype is also dependent on the MeSA esterase activity of NtSABP2 in the systemic leaves. Phenotypes, overview
malfunction
basal salicylic acid (SA) levels in Arabidopsis thaliana plants that constitutively overexpress PbBSMT compared with those in Arabidopsis wild-type Col-0 are reduced approximately 80% versus only a 50% reduction in plants overexpressing AtBSMT1. PbBSMT-overexpressing plants are more susceptible to Plasmodiophora brassicae than wild-type plants, they also are partially compromised in nonhost resistance to Albugo candida. In contrast, AtBSMT1-overexpressing plants are not more susceptible than wild-type to either Plasmodiophora brassicae or Albugo candida. Furthermore, transgenic Arabidopsis thaliana and Nicotiana tabacum plants overexpressing PbBSMT exhibit increased susceptibility to virulent Pseudomonas syringae pv. tomato DC3000 and virulent Pseudomonas syringae pv. tabaci, respectively. Gene-mediated resistance to DC3000/AvrRpt2 and tobacco mosaic virus (TMV) is also compromised in Arabidopsis thaliana and Nicotiana tabacum cv. Xanthi-nc plants overexpressing PbBSMT, respectively. Transient expression of PbBSMT or AtBSMT1 in lower leaves of Nicotiana tabacum cv. Xanthi-nc results in systemic acquired resistance (SAR)-like enhanced resistance to TMV in the distal systemic leaves. The development of a PbBSMT-mediated SAR-like phenotype is also dependent on the MeSA esterase activity of NtSABP2 in the systemic leaves. Phenotypes, overview
malfunction
for Populus class II SABATH proteins, both forward and reverse mutagenesis studies show that a single amino acid switch between PtSABATH4 and PtSABATH24 results in substrate switch. The mutation of Met156 to His results in a switch from a preference for salicylic acid (SA) over benzoic acid (BA) in wild-type PtSABATH4 to a preference for BA over SA in the M156H mutant. The mutation of His157 of PtSABATH24 (EC 2.1.1.273) to a methionine residue also results in a switch from a preference for BA over SA in wild-type PtSABATH24 to a preference for SA over BA in the H157M mutant. The PtSABATH4 mutation M314V results in decreased enzymatic activities towards both the substrates salicylic acid (SA) over benzoic acid (BA), but not in a substrate switch
malfunction
overexpression of LcSAMT gene markedly enhances the methylsalicylate (MeSA) content and reduces the accumulation of salicylate (SA) in transgenic tobacco plants, the conversion of MeSA from SA leads to the depletion of the free SA pool. Overexpression of LcSAMT gene in tobacco significantly increases sensitivity of transgenic plants to drought stress, probably due to the decreased SA accumulation. Increased accumulation of ROS, elevated MDA levels, reduced proline contents, and lowered expression of APX, CAT and SOD genes are also observed in the LcSAMT transgenic tobacco plants under drought stress, which means that the LcSAMT-overexpressing transgenic tobacco plants have decreased resistance to oxidative stress in comparison with control plants under drought stress. LcSAMT-overexpressing transgenic tobacco plants display decreased abscisic acid (ABA) accumulation and reduced transcript expression of NtNCED1 and NtRD22 genes. Therefore, the increased sensitivity of transgenic plants overexpressing LcSAMT gene to drought stress might also act through an ABA-dependent pathway. Overexpression of LcSAMT decreases RWC, proline, chlorophyll content, and the photosynthetic capacity, and increases MDA content of transgenic Nicotiana tabacum plants exposed to drought stress
malfunction
recombinant BSMT enzyme expression in Arabidopsis thaliana under the control of a dexamethasone-inducible promoter leads to chlorosis and altered host susceptibility. Transcription of PbBSMT is associated with: (1) strong leaf phenotypes from anthocyanin accumulation and chlorosis followed by browning, (2) increased plant susceptibility after infection with Plasmodiophora brassicae that is manifested as more yellow leaves and reduced growth of upper plant parts, and (3) induced transgenic plants are not able to support large galls and had a brownish appearance of some clubs. Microarray data indicate that chlorophyll loss is accompanied by reduced transcription of genes involved in photosynthesis, while genes encoding glucose metabolism, mitochondrial functions and cell wall synthesis are upregulated. Phenotype overview
malfunction
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AtBSMT1-overexpressing plants are not more susceptible than wild-type to either Plasmodiophora brassicae or Albugo candida. Transgenic Arabidopsis thaliana and Nicotiana tabacum plants overexpressing PbBSMT exhibit increased susceptibility to virulent Pseudomonas syringae pv. tomato DC3000 and virulent Pseudomonas syringae pv. tabaci, respectively. Gene-mediated resistance to DC3000/AvrRpt2 and tobacco mosaic virus (TMV) is also compromised in Arabidopsis thaliana and Nicotiana tabacum cv. Xanthi-nc plants overexpressing PbBSMT, respectively. Transient expression of PbBSMT or AtBSMT1 in lower leaves of Nicotiana tabacum Xanthi-nc results in systemic acquired resistance (SAR)-like enhanced resistance to TMV in the distal systemic leaves. The development of a PbBSMT-mediated SAR-like phenotype is also dependent on the MeSA esterase activity of NtSABP2 in the systemic leaves. Phenotypes, overview
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metabolism
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the enzyme is critical for methyl salicylate synthesis
metabolism
expression patterns of Populus SABATH genes under normal growth conditions and abiotic stress, overview
metabolism
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indole-3-acetic acid (IAA), gibberellins (GAs), salicylic acid (SA) and jasmonic acid (JA) exist in methyl ester forms in plants in addition to their free acid forms. The enzymes catalyze methylation of these carboxylic acid phytohormones occurs in form of ten isozymes, PaSABATH1-10
metabolism
the enzyme is involved in the secondary metabolic pathways leading to the formation of scent volatiles in Jasminum sambac flower, overview. Developmental pattern of emission of sent volatiles in Jasminum sambac flower on a time-course basis, and concentrations of the above benzenoids and terpenes in the flowers with respect to spatial and temporal regulation
metabolism
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the expression and activities of MeSA esterase (MES), benzoic acid/SA methyltransferase (BSMT) and starch synthase (SS 1) are presumed to be involved in the defense response and monitored. Specifically, BoMES2, BoMES4_2, BoMES9 genes might be involved in the esterase activity to form free salicylate, supporting their defense activity during fungal infection. Another gene potentially involved in the esterase activity during clubroot development is BoMES9_1. Analysis of protein interaction network, overview. BoBSMT1 shows interaction with UGT74F2 and DIR1, which can play positive regulatory roles in glucosyltransferase and SAR signaling respectively
physiological function
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isoform SAM1 plays a role in soybean defence against the soybean cyst nematode Heterodera glycines. Enzyme overexpression also affects the expression of selected genes involved in salicylic acid biosynthesis and salicylic acid signal transduction
physiological function
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isoform SAMT1 may play a dual regulation role of distinct signaling in Atropa belladonna plants, namely the signaling pathway of the SA-dependent response, and also a jasmonic acid dependent response in local regions
physiological function
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overexpression of isoform BSMT1 compromises systemic acquired resistance and pathogen-associated molecular pattern-triggered immunity but not effector-triggered immunity
physiological function
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both methyl salicylate and methyl jasmonate are essential for systemic resistance against Tobacco mosaic virus, possibly acting as the initiating signals for systemic resistance, irreplaceable roles of methyl salicylate and methyl jasmonate in systemic resistance response
physiological function
enzyme benzoic acid/salicylic acid carboxyl methyltransferase is enzyme responsible for catalyzing benzoic acid and salicylic acid to methyl benzoate and methyl salicylate, respectively, and is involved in floral scent production from lily
physiological function
enzyme benzoic acid/salicylic acid carboxyl methyltransferase is enzyme responsible for catalyzing salicylic acid and benzoic acid via salicylic acid to methyl salicylate, and is involved in plant defense against pathogens. The phenylalanine ammonia-lyase, not the isochorismate pathway, is the primary route for salicylic acid production in tomato
physiological function
the obligate biotrophic pathogen Plasmodiophora brassicae causes clubroot disease in Arabidopsis thaliana, which is characterized by large root galls. Salicylic acid production is a defence response in plants, and its methyl ester is involved in systemic signalling. Plasmodiophora brassicae suppresses the plant defence reactions via its methyltransferase, PbBSMT with homology to plant methyltransferases. The PbBSMT gene is maximally transcribed when salicylic acid production is highest, and enzyme PbBSMT can methylate salicylic acid, benzoic and anthranilic acids. Plasmodiophora brassicae secretes enzyme PbBSMT into the host cell, where it methylates the defence signal salicylate. The resulting methyl salicylate fails to upregulate plant defence reactions and is transmitted to leaves, where it is emitted or converted back to salicylate
physiological function
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Brassica oleracea var. capitata production is severely affected by clubroot disease caused by the soil-borne plant pathogen Plasmodiophora brassicae. During clubroot development, methyl salicylate (MeSA) is biosynthesized from salicylic acid (SA) by salicylate methyltransferase. Methyl salicylate esterase (MES) plays a major role in the conversion of MeSA back into free SA. Analysis of the interrelationship between MES and salicylate methytransferases during clubroot development, overview
physiological function
Brassica oleracea var. capitata production is severely affected by clubroot disease caused by the soil-borne plant pathogen Plasmodiophora brassicae. During clubroot development, methyl salicylate (MeSA) is biosynthesized from salicylic acid (SA) by salicylate methyltransferase. Methyl salicylate esterase (MES) plays a major role in the conversion of MeSA back into free SA. Analysis of the interrelationship between MES and salicylate methytransferases during clubroot development, overview
physiological function
mimicking the host regulation of salicylic acid: a virulence strategy by the clubroot pathogen Plasmodiophora brassicae, overview. The plant hormone salicylic acid (SA) plays a critical role in defense against biotrophic pathogens, e.g. Plasmodiophora brassicae, which is an obligate pathogen of crucifer species and the causal agent of clubroot disease of canola (Brassica napus), encoding a protein with very limited homology to benzoic acid (BA)/SA-methyltransferase, designated PbBSMT. Enzyme PbBSMT is an effector, which is secreted by Plasmodiophora brassicae into its host plant to deplete pathogen-induced SA accumulation. Plasmodiophora brassicae uses PbBSMTto overcome SA-mediated defenses by converting SA into inactive methyl salicylate (MeSA). PbBSMT suppresses local defense and provide evidence that PbBSMT is much more effective than endogenous Arabidopsis thaliana host enzyme AtBSMT1 at suppressing the levels of SA and its associated effects. PbBSMT is much more effective than AtBSMT1 at both reducing endogenous and exogenous SA levels and at suppressing multiple levels of resistance, including nonhost and basal resistance as well as pattern-triggered immunity (PTI) and effector-triggered immunity (ETI)
physiological function
mimicking the host regulation of salicylic acid: a virulence strategy by the clubroot pathogen Plasmodiophora brassicae, overview. The plant hormone salicylic acid (SA) plays a critical role in defense against biotrophic pathogens, e.g. Plasmodiophora brassicae, which is an obligate pathogen of crucifer species and the causal agent of clubroot disease of canola (Brassica napus). A pathogen salicylate methyltransferase, PbBSMT, suppresses local defense and provide evidence that PbBSMT is much more effective than endogenous Arabidopsis thaliana host methyltransferase enzyme AtBSMT1 at suppressing the levels of SA and its associated effects. PbBSMT is much more effective than AtBSMT1 at both reducing endogenous and exogenous SA levels and at suppressing multiple levels of resistance, including nonhost and basal resistance as well as pattern-triggered immunity (PTI) and effector-triggered immunity (ETI)
physiological function
salicylic acid (SA) is a phenolic compound involved in plant growth and development. Salicylic acid carboxyl methyltransferase (SAMT) can catalyze the methylation of SA with S-adenosyl-L-methionine as the methyl donor to form methyl salicylate (MeSA). Recombinant salicylic acid carboxyl methyltransferase-like gene LcSAMT from Lycium chinense negatively regulates the drought response in transgenic tobacco. Enzyme LcSAMT regulates the expression of stress-related genes in transgenic Nicotiana tabacum plants exposed to drought stress
physiological function
salicylic acid carboxyl methyltransferase activity from Camellia sinensis provides the aroma compound methyl salicylate (MeSA) during the withering process of white tea. During the withering process for white tea producing, MeSA is generated by salicylic acid carboxyl methyltransferase (SAMT) with salicylic acid (SA), and the specific floral scent is formed
physiological function
the enzyme is involved in enzymatic production and emission of floral scent volatiles in Jasminum sambac
physiological function
the plant pathogenic protist Plasmodiophora brassicae causes clubroot disease of Brassicaceae. The biotrophic organism can downregulate plant defence responses via its salicylic acid methyltransferase. The enzyme is involved in attenuation of host defence responses in the roots by metabolising a plant defence signal. Role for the methylation of salicylic acid in attenuating plant defence response in infected roots as a strategy for intracellular parasitism. Salicylic acid (SA) is a plant defence hormone that acts as a prominent signal in response to biotrophic pathogens
physiological function
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mimicking the host regulation of salicylic acid: a virulence strategy by the clubroot pathogen Plasmodiophora brassicae, overview. The plant hormone salicylic acid (SA) plays a critical role in defense against biotrophic pathogens, e.g. Plasmodiophora brassicae, which is an obligate pathogen of crucifer species and the causal agent of clubroot disease of canola (Brassica napus). A pathogen salicylate methyltransferase, PbBSMT, suppresses local defense and provide evidence that PbBSMT is much more effective than endogenous Arabidopsis thaliana host methyltransferase enzyme AtBSMT1 at suppressing the levels of SA and its associated effects. PbBSMT is much more effective than AtBSMT1 at both reducing endogenous and exogenous SA levels and at suppressing multiple levels of resistance, including nonhost and basal resistance as well as pattern-triggered immunity (PTI) and effector-triggered immunity (ETI)
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additional information
analysis of molecular mechanism of LcSAMT gene
additional information
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differences in susceptibility to Plasmodiophora brassicae are characterized based on presence or absence of root galls in the two lines of Brassica oleracea
additional information
differences in susceptibility to Plasmodiophora brassicae are characterized based on presence or absence of root galls in the two lines of Brassica oleracea
additional information
three-dimensional structure modeling of PtSABATH4 based on the 1M6E crystal structure. Similar to 1M6E, residues Met156 and Met314 of PtSABATH4 also create a molecular clamp that encompasses the benzyl ring of salicylate
additional information
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three-dimensional structure modeling of PtSABATH4 based on the 1M6E crystal structure. Similar to 1M6E, residues Met156 and Met314 of PtSABATH4 also create a molecular clamp that encompasses the benzyl ring of salicylate
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Clarkia breweri SAMT cloned into expression vector pET28a(+) and construct transformed into Escherichia coli BL21(DE3) cells
coding regions of AlBSMT1 ligated into pCRT7/CT-TOPO TA vector for functional expression in Escherichia coli
coding regions of AtBSMT1 ligated into pCRT7/CT-TOPO TA vector for functional expression in Escherichia coli
expressed in Escherichia coli BL21(DE3) CodonPlus cells
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expressed in Escherichia coli BL21-AI cells
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gene BSMT, cloning in Escherichia coli, Arabidopsis thaliana plants are transformed using the floral dip method via Agrobacterium tumefaciens AGL1, recombinant BSMT enzyme expression in Arabidopsis thaliana under the control of a dexamethasone-inducible promoter leading to chlorosis and altered host susceptibility, induced transgenic plants are not able to support large galls and have a brownish appearance of some clubs. The methylester of SA (MeSA) is transported from clubbed Arabidopsis roots to leaves, as shown using heavy isotope-labelled MeSA, and is emitted only from leaves of infected plants, semi- and quantitative RT-PCR expression analysis
gene BSMT, real-time PCR enzyme expression analysis in Plasmodiophora brassicae-infected Brassica oleracea lines
gene BSMT, recombinant expression of 35S::PbBSMT in planta in Arabidopsis thaliana reduces salicylate (SA) levels and increases susceptibility to clubroot, Plasmodiophora brassicae
gene LiBSMT, DNA and amino acid sequence determination and analysis, sequence comparison and phylogenetic analysis and tree, quantitative real-time PCR expression analysis, recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)
gene NbSAMT, quantitative real-time PCR enzyme expression analysis
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gene PbBSMT, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) codon plus
gene SABATH4, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, overview, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
gene SAMT, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, functional recombinant expression in Escherichia coli, and functional recombinant expression in transgenic Nicotiana tabacum plants via Agrobacterium tunefaciens strain EHA105 transfection method, overexpression of LcSAMT gene markedly enhances the methylsalicylate content and reduces the accumulation of salicylate in transgenic tobacco plants
gene SAMT, sequence comparisons, regulatory elements in the cloned CsSAMT promoter sequence, real-time quantitative PCR enzyme expression analysis, recombinant expression in Escherichia coli and in Saccharomyces cerevisiae
genes PsSABATH2, DNA and amino acid sequence determination and analysis, sequence comparisons, genetic organization and localization of SABATH genes PsSABATH1-10 in the genome of Picea abies, overview. Sequence similarities among PaSABATHs range from 49% to 91%. Most PaSABATH genes have three introns with the exception of PaSABATH4, PaSABATH5 and PaSABATH10, each of which contains two introns. Phylogenetic analysis and tree
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recombinant expression in Escherichia coli strain BL21(DE3)
SAMT cDNA expressed with pET-11a/pET-28 vector in Escherichia coli which synthesizes a functional non-tagged/His-tagged SAMT protein
subcloned into expression vector pET-28a, containing an N-terminal polyhistidine 6-His-tag, and expressed in Escherichia coli
gene BSMT, real-time PCR enzyme expression analysis in Plasmodiophora brassicae-infected Brassica oleracea lines
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gene BSMT, real-time PCR enzyme expression analysis in Plasmodiophora brassicae-infected Brassica oleracea lines
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Ross, J.R.; Nam, K.H.; D'Auria, J.C.; Pichersky, E.
S-Adenosyl-L-methionine:salicylic acid carboxyl methyltransferase, an enzyme involved in floral scent production and plant defense, represents a new class of plant methyltransferases
Arch. Biochem. Biophys.
367
9-16
1999
Clarkia breweri (Q9SPV4)
brenda
Negre, F.; Kolosova, N.; Knoll, J.; Kish, C.M.; Dudareva, N.
Novel S-adenosyl-L-methionine:salicylic acid carboxyl methyltransferase, an enzyme responsible for biosynthesis of methyl salicylate and methyl benzoate, is not involved in floral scent production in snapdragon flowers
Arch. Biochem. Biophys.
406
261-270
2002
Antirrhinum majus (Q8H6N2), Antirrhinum majus
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Zubieta, C.; Ross, J.R.; Koscheski, P.; Yang, Y.; Pichersky, E.; Noel, J.P.
Structural basis for substrate recognition in the salicylic acid carboxyl methyltransferase family
Plant Cell
15
1704-1716
2003
Clarkia breweri (Q9SPV4), Clarkia breweri
brenda
Chen, F.; D'Auria, J.C.; Tholl, D.; Ross, J.R.; Gershenzon, J.; Noel, J.P.; Pichersky, E.
An Arabidopsis thaliana gene for methylsalicylate biosynthesis, identified by a biochemical genomics approach, has a role in defense
Plant J.
36
577-588
2003
Arabidopsis lyrata (Q6XMI1), Arabidopsis thaliana (Q6XMI3)
brenda
Yao, J.; Xu, Q.; Chen, F.; Guo, H.
QM/MM free energy simulations of salicylic acid methyltransferase: effects of stabilization of TS-like structures on substrate specificity
J. Phys. Chem. B
115
389-396
2011
Clarkia breweri
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Liu, P.P.; Yang, Y.; Pichersky, E.; Klessig, D.F.
Altering expression of benzoic acid/salicylic acid carboxyl methyltransferase 1 compromises systemic acquired resistance and PAMP-triggered immunity in Arabidopsis
Mol. Plant Microbe Interact.
23
82-90
2010
Arabidopsis thaliana
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Lin, J.; Mazarei, M.; Zhao, N.; Zhu, J.J.; Zhuang, X.; Liu, W.; Pantalone, V.R.; Arelli, P.R.; Stewart, C.N.; Chen, F.
Overexpression of a soybean salicylic acid methyltransferase gene confers resistance to soybean cyst nematode
Plant Biotechnol. J.
11
1135-1145
2013
Glycine max
brenda
Kwon, S.; Hamada, K.; Matsuyama, A.; Yasuda, M.; Nakashita, H.; Yamakawa, T.
Biotic and abiotic stresses induce AbSAMT1, encoding S-adenosyl-L-methionine: salicylic acid carboxyl methyltransferase, in Atropa belladonna
Plant Biotechnol.
26
207-215
2009
Atropa belladonna
-
brenda
Tieman, D.; Zeigler, M.; Schmelz, E.; Taylor, M.G.; Rushing, S.; Jones, J.B.; Klee, H.J.
Functional analysis of a tomato salicylic acid methyl transferase and its role in synthesis of the flavor volatile methyl salicylate
Plant J.
62
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2010
Solanum lycopersicum
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Wang, H.; Sun, M.; Li, L.L.; Xie, X.H.; Zhang, Q.X.
Cloning and characterization of a benzoic acid/salicylic acid carboxyl methyltransferase gene involved in floral scent production from lily (Lilium Yelloween)
Genet. Mol. Res.
14
14510-14521
2015
Lilium hybrid cultivar (A0A075W3C7)
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Krol, P.; Igielski, R.; Pollmann, S.; Kepczynska, E.
Priming of seeds with methyl jasmonate induced resistance to hemi-biotroph Fusarium oxysporum f.sp. lycopersici in tomato via 12-oxo-phytodienoic acid, salicylic acid, and flavonol accumulation
J. Plant Physiol.
179
122-132
2015
Solanum lycopersicum (D2Y3T9)
brenda
Zhu, F.; Xi, D.H.; Yuan, S.; Xu, F.; Zhang, D.W.; Lin, H.H.
Salicylic acid and jasmonic acid are essential for systemic resistance against tobacco mosaic virus in Nicotiana benthamiana
Mol. Plant Microbe Interact.
27
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2014
Nicotiana benthamiana
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Ludwig-Mueller, J.; Juelke, S.; Geiss, K.; Richter, F.; Mithoefer, A.; ?ola, I.; Rusak, G.; Keenan, S.; Bulman, S.
A novel methyltransferase from the intracellular pathogen Plasmodiophora brassicae methylates salicylic acid
Mol. Plant Pathol.
16
349-364
2015
Plasmodiophora brassicae (R4I7S9), Plasmodiophora brassicae
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Bera, P.; Mukherjee, C.; Mitra, A.
Enzymatic production and emission of floral scent volatiles in Jasminum sambac
Plant Sci.
256
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2017
Jasminum sambac (A0A0A1E7P5), Jasminum sambac
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Wang, G.; Li, Q.; Wang, C.; Jin, C.; Ji, J.; Guan, C.
A salicylic acid carboxyl methyltransferase-like gene LcSAMT from Lycium chinense, negatively regulates the drought response in transgenic tobacco
Environ. Exp. Bot.
167
103833
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Lycium chinense (A0A514TTE2)
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Akhtar, M.K.; Vijay, D.; Umbreen, S.; McLean, C.J.; Cai, Y.; Campopiano, D.J.; Loake, G.J.
Hydrogen peroxide-based fluorometric assay for real-time monitoring of SAM-dependent methyltransferases
Front. Bioeng. Biotechnol.
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Clarkia breweri (Q9SPV4)
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Manoharan, R.K.; Shanmugam, A.; Hwang, I.; Park, J.I.; Nou, I.S.
Expression of salicylic acid-related genes in Brassica oleracea var. capitata during Plasmodiophora brassicae infection
Genome
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2016
Brassica oleracea var. capitata, Plasmodiophora brassicae (R4I7S9)
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Deng, W.W.; Wang, R.; Yang, T.; Jiang, L.; Zhang, Z.Z.
Functional characterization of salicylic acid carboxyl methyltransferase from Camellia sinensis, providing the aroma compound of methyl salicylate during the withering process of white tea
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Camellia sinensis (A0A167V6N5), Camellia sinensis
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Djavaheri, M.; Ma, L.; Klessig, D.F.; Mithoefer, A.; Gropp, G.; Borhan, H.
Mimicking the host regulation of salicylic acid a virulence strategy by the clubroot pathogen Plasmodiophora brassicae
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Arabidopsis thaliana (Q6XMI3), Plasmodiophora brassicae (R4I7S9), Arabidopsis thaliana Col-0 (Q6XMI3)
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Chaiprasongsuk, M.; Zhang, C.; Qian, P.; Chen, X.; Li, G.; Trigiano, R.N.; Guo, H.; Chen, F.
Biochemical characterization in Norway spruce (Picea abies) of SABATH methyltransferases that methylate phytohormones
Phytochemistry
149
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2018
Picea abies
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Bulman, S.; Richter, F.; Marschollek, S.; Benade, F.; Juelke, S.; Ludwig-Mueller, J.
Arabidopsis thaliana expressing PbBSMT, a gene encoding a SABATH-type methyltransferase from the plant pathogenic protist Plasmodiophora brassicae, show leaf chlorosis and altered host susceptibility
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Plasmodiophora brassicae (R4I7S9)
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Han, X.; Yang, Q.; Liu, Y.; Yang, Z.; Wang, X.; Zeng, Q.; Yang, H.
Evolution and function of the Populus SABATH family reveal that a single amino acid change results in a substrate switch
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Populus trichocarpa (A9PF83), Populus trichocarpa
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