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S-adenosyl-L-methionine + 3-hydroxybenzoate
methyl 3-hydroxybenzoate + S-adenosyl-L-homocysteine
26% activity compared to salicylate
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S-adenosyl-L-methionine + 3-hydroxybenzoate
S-adenosyl-L-homocysteine + methyl 3-hydroxybenzoate
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1.8% activity compared to salicylate
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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
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2% activity compared to salicylate
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S-adenosyl-L-methionine + 4-hydroxybenzoate
S-adenosyl-L-homocysteine + methyl 4-hydroxybenzoate
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lower catalytic efficiency with 4-hydroxybenzoate compared to salicylate
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S-adenosyl-L-methionine + anthranilate
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9.3% activity compared to salicylate
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S-adenosyl-L-methionine + anthranilate
methyl anthranilate + S-adenosyl-L-homocysteine
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S-adenosyl-L-methionine + anthranilic acid
S-adenosyl-L-homocysteine + methyl anthranilate
S-adenosyl-L-methionine + benzoate
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16.9% activity compared to salicylate
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S-adenosyl-L-methionine + benzoate
methyl benzoate + S-adenosyl-L-homocysteine
S-adenosyl-L-methionine + benzoate
S-adenosyl-L-homocysteine + methyl benzoate
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2% activity compared to salicylate
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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%
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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
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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
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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
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additional information
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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%
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?
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%
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S-adenosyl-L-methionine + 3-hydroxybenzoic acid
S-adenosyl-L-homocysteine + methyl 3-hydroxybenzoate
17% activity of wild-type enzyme compared to salicylate methylation
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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%
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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%
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?
S-adenosyl-L-methionine + benzoate
methyl benzoate + S-adenosyl-L-homocysteine
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S-adenosyl-L-methionine + benzoate
methyl benzoate + S-adenosyl-L-homocysteine
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S-adenosyl-L-methionine + benzoate
methyl benzoate + S-adenosyl-L-homocysteine
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S-adenosyl-L-methionine + benzoate
methyl benzoate + S-adenosyl-L-homocysteine
96% activity compared to salicylate
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S-adenosyl-L-methionine + benzoate
methyl benzoate + S-adenosyl-L-homocysteine
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S-adenosyl-L-methionine + benzoate
methyl benzoate + S-adenosyl-L-homocysteine
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8% activity compared to salicylate
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S-adenosyl-L-methionine + benzoate
methyl benzoate + S-adenosyl-L-homocysteine
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S-adenosyl-L-methionine + benzoate
methyl benzoate + S-adenosyl-L-homocysteine
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S-adenosyl-L-methionine + salicylate
methyl salicylate + S-adenosyl-L-homocysteine
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S-adenosyl-L-methionine + salicylate
methyl salicylate + S-adenosyl-L-homocysteine
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S-adenosyl-L-methionine + salicylate
methyl salicylate + S-adenosyl-L-homocysteine
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S-adenosyl-L-methionine + salicylate
methyl salicylate + S-adenosyl-L-homocysteine
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S-adenosyl-L-methionine + salicylate
methyl salicylate + S-adenosyl-L-homocysteine
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S-adenosyl-L-methionine + salicylate
methyl salicylate + S-adenosyl-L-homocysteine
best substrate
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S-adenosyl-L-methionine + salicylate
methyl salicylate + S-adenosyl-L-homocysteine
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S-adenosyl-L-methionine + salicylate
methyl salicylate + S-adenosyl-L-homocysteine
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S-adenosyl-L-methionine + salicylate
methyl salicylate + S-adenosyl-L-homocysteine
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S-adenosyl-L-methionine + salicylate
methyl salicylate + S-adenosyl-L-homocysteine
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best substrate
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S-adenosyl-L-methionine + salicylate
methyl salicylate + S-adenosyl-L-homocysteine
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S-adenosyl-L-methionine + salicylate
methyl salicylate + S-adenosyl-L-homocysteine
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S-adenosyl-L-methionine + salicylate
S-adenosyl-L-homocysteine + methyl salicylate
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S-adenosyl-L-methionine + salicylate
S-adenosyl-L-homocysteine + methyl salicylate
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S-adenosyl-L-methionine + salicylate
S-adenosyl-L-homocysteine + methyl salicylate
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S-adenosyl-L-methionine + salicylate
S-adenosyl-L-homocysteine + methyl salicylate
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S-adenosyl-L-methionine + salicylate
S-adenosyl-L-homocysteine + methyl salicylate
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highest level of specific activity with salicylate
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S-adenosyl-L-methionine + salicylate
S-adenosyl-L-homocysteine + methyl salicylate
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S-adenosyl-L-methionine + salicylate
S-adenosyl-L-homocysteine + methyl salicylate
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S-adenosyl-L-methionine + salicylate
S-adenosyl-L-homocysteine + methyl salicylate
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S-adenosyl-L-methionine + salicylate
S-adenosyl-L-homocysteine + methyl salicylate
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S-adenosyl-L-methionine + salicylate
S-adenosyl-L-homocysteine + methyl salicylate
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100% activity
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S-adenosyl-L-methionine + salicylic acid
S-adenosyl-L-homocysteine + methyl salicylate
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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%
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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%
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additional information
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enzyme is also active with benzoic acid resulting in methyl benzoate formation
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additional information
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enzyme is also active with benzoic acid resulting in methyl benzoate formation
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additional information
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no activity with 3-hydroxybenzoic acid, 4-hydroxybenzoic acid, trans-cinnamic acid, p-coumaric acid, m-coumaric acid, o-coumaric acid and benzyl alcohol
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additional information
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no activity with 3-hydroxybenzoic acid, 4-hydroxybenzoic acid, trans-cinnamic acid, p-coumaric acid, m-coumaric acid, o-coumaric acid and benzyl alcohol
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additional information
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enzyme is also active with benzoic acid resulting in methyl benzoate formation
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additional information
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in contrast to AtBSMT1 no activity with 1 mM 3-hydroxybenzoic acid
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additional information
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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
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enzyme is also active with benzoic acid resulting in methyl benzoate formation
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additional information
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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
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substrate specificity of recombinant enzyme, overview
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additional information
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substrate specificity of recombinant enzyme, overview
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additional information
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enzyme is also active with benzoic acid resulting in methyl benzoate formation
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additional information
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no activity with 4-hydroxybenzoic acid, vanillic acid, caffeic acid, p-coumaric acid and (+/-)jasmonic acid
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additional information
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no measurable methylation of jasmonic acid by wild-type SAMT using concentrations up to 5 mM
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additional information
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no measurable methylation of jasmonic acid by wild-type SAMT using concentrations up to 5 mM
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additional information
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wild-type is also able to methylate benzoic acid with 48% activity compared to salicylate methylation
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additional information
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wild-type is also able to methylate benzoic acid with 48% activity compared to salicylate methylation
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additional information
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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
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additional information
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jasmonic acid, indole-3-acetic acid and gibberellic acid do not serve as substrates for isoform SAMT1
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additional information
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GC-MS product identification
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additional information
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GC-MS product identification
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additional information
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the enzyme also catalyzes the reaction of benzoic acid carboxyl methyltransferase, EC 2.1.1.273
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additional information
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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
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additional information
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the enzyme also catalyzes the reaction of benzoic acid carboxyl methyltransferase, EC 2.1.1.273
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additional information
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the enzyme also catalyzes the reaction of benzoic acid carboxyl methyltransferase, EC 2.1.1.273
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additional information
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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
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additional information
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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
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additional information
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less than 1% activity with jasmonic acid, indole-3-acetic acid and gibberellic acid 3
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