2.1.1.274: salicylate 1-O-methyltransferase
This is an abbreviated version!
For detailed information about salicylate 1-O-methyltransferase, go to the full flat file.
Reaction
Synonyms
AlBSMT1, AtBSMT1, benzoate-salicylate methyltransferase, benzoic acid/SA methyltransferase, benzoic acid/salicylic acid carboxyl methyltransferase, benzoic acid/salicylic acid carboxyl methyltransferase 1, benzoic acid/salicylic acid methyltransferase, benzoic acid/salicylic acidcarboxyl methyltransferase, BSMT, BSMT1, class II SABATH protein, CsSAMT, LcSAMT, More, PaSABATH2, PaSAMT, PbBSMT methyltransferase, PtSABATH4, S-adenosyl-l-methionine: salicylic acid carboxyl methyl-transferase, S-adenosyl-L-methionine: salicylic acid carboxyl methyltransferase, S-adenosyl-L-methionine:salicylic acid carboxyl methyltransferase, SA carboxyl methyltransferase, SA methyl transferase, SA methyltransferase, SA MTase, SABATH methyltransferase 4, SABATH4, salicylic acid carboxyl methyltransferase, salicylic acid carboxyl methyltransferase-like, salicylic acid methyl transferase, salicylic acid methyltransferase, salicylicacid carboxyl methyl transferase, SAMT, SAMT1
ECTree
2.1.1.274 salicylate 1-O-methyltransferaseAdvanced search results
results (
results (Engineering
Engineering on EC 2.1.1.274 - salicylate 1-O-methyltransferase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Y147S
reduced methylation of benzoic acid and 3-hydroxybenzoic acid but slightly increased activity towards jasmonic acid
Y147S/M150H
significant increase in the ability to turn over jasmonic acid and vanillic acid
Y147S/M150H/F347Y
slightly increased activity towards short-chain carboxylic acids and jasmonic acid
Y147S/M150H/F347Y/N349I
highly increased activity towards short-chain carboxylic acids and aromatic acids like hydroxybenzoic acids, vanillic acid, jasmonic acid, cinnamic acid, 4-coumaric acid and caffeic acid, broadest substrate spectrum
Y147S/M150H/I225Q/F347Y
greatest specific activities against 3-hydroxybenzoic acid, vanillic acid and jasmonic acid but reduced activity towards salicylic acid
M156H
site-directed mutagenesis, 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
M314V
site-directed mutagenesis, the mutation results in decreased enzymatic activities towards both the substrates salicylic acid (SA) over benzoic acid (BA), but not in a substrate switch
additional information
additional information
an AtBSMT1 T-DNA knockout (AtBSMT1 KO, SALK_140496) is transformed by AtBSMT1 (Ask6) and PbBSMT (PsK5) and their susceptibility to clubroot is assessed. The infection rate is similar in the AtBSMT1 KO and AsK6 and comparable to that in wild-type. In contrast, PsK5 plants produce significantly larger galls than produced by the AtBSMT1 knockout
additional information
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an AtBSMT1 T-DNA knockout (AtBSMT1 KO, SALK_140496) is transformed by AtBSMT1 (Ask6) and PbBSMT (PsK5) and their susceptibility to clubroot is assessed. The infection rate is similar in the AtBSMT1 KO and AsK6 and comparable to that in wild-type. In contrast, PsK5 plants produce significantly larger galls than produced by the AtBSMT1 knockout
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additional information
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silencing of gene NbSAMT, quantitative real-time PCR defense-related genes expression analysis
additional information
an AtBSMT1 T-DNA knockout (AtBSMT1 KO, SALK_140496) is transformed by AtBSMT1 (Ask6) and PbBSMT (PsK5) and their susceptibility to clubroot is assessed. The infection rate is similar in the AtBSMT1 KO and AsK6 and comparable to that in wild-type. In contrast, PsK5 plants produce significantly larger galls than produced by the AtBSMT1 knockout
