Literature summary for 2.1.1.273 extracted from

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 (2018), Front. Bioeng. Biotechnol., 6, 146 .

Search for more literature for 2.1.1.273

Cloned(Commentary)

Cloned (Comment)	Organism
recombinant expression in Escherichia coli strain BL21(DE3)	Clarkia breweri

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.0068	-	salicylate	pH 7.5, 30°C	Clarkia breweri

Metals/Ions

Metals/Ions	Comment	Organism	Structure
KCl	activates at 1 mM	Clarkia breweri

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
S-adenosyl-L-methionine + salicylate	Clarkia breweri	-	methyl salicylate + S-adenosyl-L-homocysteine	-	?

Organism

Organism	UniProt	Comment	Textmining
Clarkia breweri	Q9SPV4	i.e. Eucharidium breweri	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	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	?	-	-
S-adenosyl-L-methionine + 3-hydroxybenzoate	26% activity compared to salicylate	Clarkia breweri	methyl 3-hydroxybenzoate + S-adenosyl-L-homocysteine	-	?
S-adenosyl-L-methionine + benzoate	96% activity compared to salicylate	Clarkia breweri	methyl benzoate + S-adenosyl-L-homocysteine	-	?
S-adenosyl-L-methionine + salicylate	-	Clarkia breweri	methyl salicylate + S-adenosyl-L-homocysteine	-	?
S-adenosyl-L-methionine + salicylate	best substrate	Clarkia breweri	methyl salicylate + S-adenosyl-L-homocysteine	-	?
S-adenosyl-L-methionine + vanillate	12% activity compared to salicylate	Clarkia breweri	methyl vanillate + S-adenosyl-L-homocysteine	-	?

Synonyms

Synonyms	Comment	Organism
More	see also EC 2.1.1.274	Clarkia breweri
SA MTase	-	Clarkia breweri
salicylic acid methyltransferase	-	Clarkia breweri

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
30	-	assay at	Clarkia breweri

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
0.0163	-	salicylate	pH 7.5, 30°C	Clarkia breweri

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7.5	-	assay at	Clarkia breweri

Cofactor

Cofactor	Comment	Organism	Structure
S-adenosyl-L-methionine	-	Clarkia breweri

kcat/KM [mM/s]

kcat/KM Value [1/mMs^-1]	kcat/KM Value Maximum [1/mMs^-1]	Substrate	Comment	Organism	Structure
2.4	-	salicylate	pH 7.5, 30°C	Clarkia breweri

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Release 2023.1 (January 2023)