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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
?
-
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
-
-
-
?
S-adenosyl-L-methionine + benzoate
methyl benzoate + S-adenosyl-L-homocysteine
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-
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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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-
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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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-
-
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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
-
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
-
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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-
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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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?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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 + salicylate
methyl salicylate + S-adenosyl-L-homocysteine
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 + 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
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
-
-
-
-
?
S-adenosyl-L-methionine + benzoate
S-adenosyl-L-homocysteine + methyl benzoate
-
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
-
-
-
?
S-adenosyl-L-methionine + benzoate
S-adenosyl-L-homocysteine + methyl benzoate
-
-
-
-
?
S-adenosyl-L-methionine + benzoate
S-adenosyl-L-homocysteine + methyl benzoate
-
-
-
?
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
-
-
-
?
additional information
?
-
the enzyme also catalyzes the reaction of salicylate 1-O-methyltransferase, EC 2.1.1.274
-
-
?
additional information
?
-
the enzyme also catalyzes the reaction of salicylate 1-O-methyltransferase, EC 2.1.1.274
-
-
?
additional information
?
-
-
the enzyme also catalyzes the reaction of salicylate 1-O-methyltransferase, EC 2.1.1.274
-
-
?
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
differences in scent emission between Antirrhinum majus and Antirrhinum linkianum may be traced back to single genes involved in discrete biosynthetic reactions such as benzoic acid methylation. Thus, natural variation of this complex trait may be the result of combinations of wild-type, and loss of function alleles in different genes involved in discrete VOCs biosynthesis. The presence of active transposable elements in the genus may account for rapid evolution and instability, raising the possibility of adaptation to local pollinators. Genetic analysis of scent emission spanning three generations following a cross of Antirrhinum majus and Antirrhinum linkianum. Both species differ in the production of four volatile organic compounds (VOCS): methyl benzoate, beta-ocimene, methylcinnamate, and acetophenone. These compounds display mendelian segregations typical for a single gene or two loci in the F2 population. Loss of function allele of benzoic acid carboxymethyl transferase (BAMT), a gene involved in methylbenzoate synthesis in higher plants. The null allele is the result of a genomic insertion in the promoter region that is likely mediated by an IDLE MITE transposable element
evolution
differences in scent emission between Antirrhinum majus and Antirrhinum linkianum may be traced back to single genes involved in discrete biosynthetic reactions such as benzoic acid methylation. Thus, natural variation of this complex trait may be the result of combinations of wild-type, and loss of function alleles in different genes involved in discrete VOCs biosynthesis. The presence of active transposable elements in the genus may account for rapid evolution and instability, raising the possibility of adaptation to local pollinators. Genetic analysis of scent emission spanning three generations following a cross of Antirrhinum majus and Antirrhinum linkianum. Both species differ in the production of four volatile organic compounds (VOCS): methyl benzoate, beta-ocimene, methylcinnamate, and acetophenone. These compounds display mendelian segregations typical for a single gene or two loci in the F2 population. Loss of function allele of benzoic acid carboxymethyl transferase (BAMT), a gene involved in methylbenzoate synthesis in higher plants. The null allele is the result of a genomic insertion in the promoter region that is likely mediated by an IDLE MITE transposable element
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
evolution
-
differences in scent emission between Antirrhinum majus and Antirrhinum linkianum may be traced back to single genes involved in discrete biosynthetic reactions such as benzoic acid methylation. Thus, natural variation of this complex trait may be the result of combinations of wild-type, and loss of function alleles in different genes involved in discrete VOCs biosynthesis. The presence of active transposable elements in the genus may account for rapid evolution and instability, raising the possibility of adaptation to local pollinators. Genetic analysis of scent emission spanning three generations following a cross of Antirrhinum majus and Antirrhinum linkianum. Both species differ in the production of four volatile organic compounds (VOCS): methyl benzoate, beta-ocimene, methylcinnamate, and acetophenone. These compounds display mendelian segregations typical for a single gene or two loci in the F2 population. Loss of function allele of benzoic acid carboxymethyl transferase (BAMT), a gene involved in methylbenzoate synthesis in higher plants. The null allele is the result of a genomic insertion in the promoter region that is likely mediated by an IDLE MITE transposable element
-
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. Mutation of His157 of PtSABATH24 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 mutation M156H in PtSBATH4 (EC 2.1.1.274) 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
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
-
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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final enzyme in the biosynthesis of methyl benzoate
metabolism
expression patterns of Populus SABATH genes under normal growth conditions and abiotic stress, overview
metabolism
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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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attracting pollinators like bumblebees
physiological function
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the enzyme is responsible for biosynthesis of the volatile ester methylbenzoate in snapdragon flowers
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
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
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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
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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
genetic analysis of scent profiles. Comparison of the molecular structure of the Antirrhinum majus and Antirrhinum linkianum BAMT promoter, alignment of the two regions of the Antirrhinum majus PLE promoter and the Antirrhinum linkianum BAMT promoter showing high homology
additional information
genetic analysis of scent profiles. Comparison of the molecular structure of the Antirrhinum majus and Antirrhinum linkianum BAMT promoter, alignment of the two regions of the Antirrhinum majus PLE promoter and the Antirrhinum linkianum BAMT promoter showing high homology
additional information
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genetic analysis of scent profiles. Comparison of the molecular structure of the Antirrhinum majus and Antirrhinum linkianum BAMT promoter, alignment of the two regions of the Antirrhinum majus PLE promoter and the Antirrhinum linkianum BAMT promoter showing high homology
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BAMT cDNA expressed in Escherichia coli
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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 with an N-terminal His tag in Escherichia coli
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gene BAMT, DNA and amino acid sequence determination and analysis, genetic structure, sequence comparisons
gene BAMT, DNA and amino acid sequence determination and analysis, genetic structure, sequence comparisons, the benzoic acid carboxymethyl transferase from Antirrhinum linkianum appears to be a null allele as mRNA expression is not detected, no alternative splicing
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 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 SABATH24, 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)
recombinant expression in Escherichia coli strain BL21(DE3)
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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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
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 lyrata, Arabidopsis thaliana (Q6XMI3), Arabidopsis thaliana
brenda
Kllner, T.G.; Lenk, C.; Zhao, N.; Seidl-Adams, I.; Gershenzon, J.; Chen, F.; Degenhardt, J.
Herbivore-induced SABATH methyltransferases of maize that methylate anthranilic acid using s-adenosyl-L-methionine
Plant Physiol.
153
1795-1807
2010
Zea mays
brenda
Murfitt, L.M.; Kolosova, N.; Mann, C.J.; Dudareva, N.
Purification and characterization of S-adenosyl-L-methionine:benzoic acid carboxyl methyltransferase, the enzyme responsible for biosynthesis of the volatile ester methyl benzoate in flowers of Antirrhinum majus
Arch. Biochem. Biophys.
382
145-151
2000
Antirrhinum majus
brenda
Effmert, U.; Saschenbrecker, S.; Ross, J.; Negre, F.; Fraser, C.M.; Noel, J.P.; Dudareva, N.; Piechulla, B.
Floral benzenoid carboxyl methyltransferases: from in vitro to in planta function
Phytochemistry
66
1211-1230
2005
Antirrhinum majus, Arabidopsis thaliana, Nicotiana suaveolens, Arabidopsis lyrata
brenda
Dudareva, N.; Murfitt, L.M.; Mann, C.J.; Gorenstein, N.; Kolosova, N.; Kish, C.M.; Bonham, C.; Wood, K.
Developmental regulation of methyl benzoate biosynthesis and emission in snapdragon flowers
Plant Cell
12
949-961
2000
Clarkia breweri
brenda
Kolosova, N.; Sherman, D.; Karlson, D.; Dudareva, N.
Cellular and subcellular localization of S-adenosyl-L-methionine:benzoic acid carboxyl methyltransferase, the enzyme responsible for biosynthesis of the volatile ester methylbenzoate in snapdragon flowers
Plant Physiol.
126
956-964
2001
Antirrhinum majus
brenda
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)
brenda
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
brenda
Bera, P.; Mukherjee, C.; Mitra, A.
Enzymatic production and emission of floral scent volatiles in Jasminum sambac
Plant Sci.
256
25-38
2017
Jasminum sambac
brenda
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.
6
146
2018
Clarkia breweri (Q9SPV4), Clarkia breweri
brenda
Ruiz-Hernandez, V.; Hermans, B.; Weiss, J.; Egea-Cortines, M.
Genetic analysis of natural variation in Antirrhinum scent profiles identifies benzoic acid carboxymethyl transferase as the major locus controlling methyl benzoate synthesis
Front. Plant Sci.
8
27
2017
Antirrhinum linkianum (A0A1B1SP62), Antirrhinum majus (Q9FYZ9), Antirrhinum majus 165E (Q9FYZ9)
brenda
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
59
379-391
2016
Brassica oleracea var. capitata, Plasmodiophora brassicae (R4I7S9)
brenda
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
Mol. Plant Microbe Interact.
32
296-305
2019
Arabidopsis thaliana (Q6XMI3), Arabidopsis thaliana, Plasmodiophora brassicae (R4I7S9), Plasmodiophora brassicae, Arabidopsis thaliana Col-0 (Q6XMI3)
brenda
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
Plant Biol.
21 Suppl 1
120-130
2019
Plasmodiophora brassicae (R4I7S9), Plasmodiophora brassicae
brenda
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
Plant Cell Physiol.
59
392-403
2018
Populus trichocarpa (B9IPD3), Populus trichocarpa
brenda