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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-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 + 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
methyl benzoate + S-adenosyl-L-homocysteine
S-adenosyl-L-methionine + benzoate
S-adenosyl-L-homocysteine + methyl benzoate
S-adenosyl-L-methionine + benzoic acid
S-adenosyl-L-homocysteine + methyl benzoate
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 + vanillate
methyl vanillate + S-adenosyl-L-homocysteine
12% activity compared to salicylate
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additional information
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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
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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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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
S-adenosyl-L-homocysteine + methyl benzoate
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S-adenosyl-L-methionine + benzoate
S-adenosyl-L-homocysteine + methyl benzoate
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S-adenosyl-L-methionine + benzoate
S-adenosyl-L-homocysteine + methyl benzoate
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S-adenosyl-L-methionine + benzoate
S-adenosyl-L-homocysteine + methyl benzoate
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emission of methyl benzoate occurs in a rhythmic manner, with maximum emission during the day, correlating with pollinator activity
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S-adenosyl-L-methionine + benzoate
S-adenosyl-L-homocysteine + methyl benzoate
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methyl benzoate is the most abundant scent compound detected in the majority of snapdragon varieties
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S-adenosyl-L-methionine + benzoate
S-adenosyl-L-homocysteine + methyl benzoate
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S-adenosyl-L-methionine + benzoate
S-adenosyl-L-homocysteine + methyl benzoate
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S-adenosyl-L-methionine + benzoate
S-adenosyl-L-homocysteine + methyl benzoate
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S-adenosyl-L-methionine + benzoate
S-adenosyl-L-homocysteine + methyl benzoate
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S-adenosyl-L-methionine + benzoic acid
S-adenosyl-L-homocysteine + methyl benzoate
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S-adenosyl-L-methionine + benzoic acid
S-adenosyl-L-homocysteine + methyl benzoate
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S-adenosyl-L-methionine + benzoic acid
S-adenosyl-L-homocysteine + methyl benzoate
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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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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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additional information
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enzyme is also active with salicylic acid resulting in methyl salicylate formation
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additional information
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enzyme is also active with salicylic acid resulting in methyl salicylate 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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no activity toward other naturally occurring substrates like salicylic acid, trans-cinnamic acid, and their derivatives 3-hydroxybenzoic acid, 4-hydroxybenzoic acid, benzyl alcohol, and 2-coumaric, 3-coumaric, and 4-coumaric acid
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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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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 2.1.1.274, salicylate 1-O-methyltransferase
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additional information
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The enzyme, which is found in flowering plants, also has the activity of EC 2.1.1.274, salicylate 1-O-methyltransferase
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additional information
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The enzyme, which is found in flowering plants, also has the activity of EC 2.1.1.274, salicylate 1-O-methyltransferase
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additional information
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The enzyme, which is found in flowering plants, also has the activity of EC 2.1.1.274, salicylate 1-O-methyltransferase
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additional information
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no activity detected with salicylic acid and trans-cinnamic acid and their derivatives 3-hydroxybenzoic acid, 4-hydroxybenzoic acid, benzyl alcohol, and 2-,3- and 4-coumaric acid
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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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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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GC-MS product identification
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additional information
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the enzyme also catalyzes the reaction of salicylate 1-O-methyltransferase, EC 2.1.1.274
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additional information
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the enzyme also catalyzes the reaction of salicylate 1-O-methyltransferase, EC 2.1.1.274
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additional information
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the enzyme also catalyzes the reaction of salicylate 1-O-methyltransferase, EC 2.1.1.274
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additional information
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enzyme PtSABATH24 has a wide substrate spectrum, exhibiting enzymatic activity towards eight of the substrates tested, i.e. indole-3-acetic acid, benzoic acid, salicylic acid, vanillic acid, farnesoic acid, nicotinic acid, coumalic acid, and trans-cinnamic acid, with the highest enzymatic activity towards benzoic acid. Compared with other Populus SABATH proteins, PtSABATH24 shows at least 42.5fold higher enzymatic activity towards benzoic acid
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additional information
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enzyme PtSABATH24 has a wide substrate spectrum, exhibiting enzymatic activity towards eight of the substrates tested, i.e. indole-3-acetic acid, benzoic acid, salicylic acid, vanillic acid, farnesoic acid, nicotinic acid, coumalic acid, and trans-cinnamic acid, with the highest enzymatic activity towards benzoic acid. Compared with other Populus SABATH proteins, PtSABATH24 shows at least 42.5fold higher enzymatic activity towards benzoic acid
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additional information
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no activity with anthranilic acid, salicylic acid, cinnamic acid, and coumaric acid
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