EC Number   |
Substrates |
Organism |
Products |
Reversibility |
|---|
   2.1.1.274 | more |
jasmonic acid, indole-3-acetic acid and gibberellic acid do not serve as substrates for isoform SAMT1 |
Glycine max |
? |
- |
? |
| 2.1.1.274 | more |
less than 1% activity with jasmonic acid, indole-3-acetic acid and gibberellic acid 3 |
Solanum lycopersicum |
? |
- |
? |
| 2.1.1.274 | more |
no measurable methylation of jasmonic acid by wild-type SAMT using concentrations up to 5 mM |
Clarkia breweri |
? |
- |
? |
| 2.1.1.274 | more |
wild-type is also able to methylate benzoic acid with 48% activity compared to salicylate methylation |
Clarkia breweri |
? |
- |
? |
| 2.1.1.274 | more |
the enzyme also catalyzes the reaction of benzoic acid carboxyl methyltransferase, EC 2.1.1.273 |
Lilium hybrid cultivar |
? |
- |
? |
| 2.1.1.274 | more |
the enzyme also catalyzes the reaction of benzoic acid carboxyl methyltransferase, EC 2.1.1.273 |
Plasmodiophora brassicae |
? |
- |
? |
| 2.1.1.274 | more |
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 |
Clarkia breweri |
? |
- |
- |
| 2.1.1.274 | more |
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 |
Populus trichocarpa |
? |
- |
- |
| 2.1.1.274 | more |
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 |
Picea abies |
? |
- |
- |
| 2.1.1.274 | more |
substrate specificity of recombinant enzyme, overview |
Camellia sinensis |
? |
- |
- |
