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Literature summary extracted from

  • Zubieta, C.; Ross, J.R.; Koscheski, P.; Yang, Y.; Pichersky, E.; Noel, J.P.
    Structural basis for substrate recognition in the salicylic acid carboxyl methyltransferase family (2003), Plant Cell, 15, 1704-1716.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.1.1.274 Clarkia breweri SAMT cloned into expression vector pET28a(+) and construct transformed into Escherichia coli BL21(DE3) cells Clarkia breweri
2.1.1.278 expression in Escherichia coli Arabidopsis thaliana

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.1.1.274 overall structure of SAMT monomer consists of a globular domain containing the extended beta-sheet characteristic of other SAM-dependent methyltransferases and a unique alpha-helical cap that forms the top one-third of the active site cavity Clarkia breweri
2.1.1.274 SAMT crystallized from ammonium sulfate solution, model spanned the entire 359 residues of full-length Clarkia SAMT Clarkia breweri

Protein Variants

EC Number Protein Variants Comment Organism
2.1.1.274 Y147S reduced methylation of benzoic acid and 3-hydroxybenzoic acid but slightly increased activity towards jasmonic acid Clarkia breweri
2.1.1.274 Y147S/M150H significant increase in the ability to turn over jasmonic acid and vanillic acid Clarkia breweri
2.1.1.274 Y147S/M150H/F347Y slightly increased activity towards short-chain carboxylic acids and jasmonic acid Clarkia breweri
2.1.1.274 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 Clarkia breweri
2.1.1.274 Y147S/M150H/I225Q/F347Y greatest specific activities against 3-hydroxybenzoic acid, vanillic acid and jasmonic acid but reduced activity towards salicylic acid Clarkia breweri

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.1.1.274 0.023
-
 salicylate wild type enzyme, pH 7.5, 25°C Clarkia breweri
2.1.1.278 0.013
-
 (indol-3-yl)acetate pH 7.5, 25°C Arabidopsis thaliana

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.1.1.278 Mg2+ binds Mg2+ Arabidopsis thaliana

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.1.1.274 41000
-
 SDS-PAGE Clarkia breweri

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.1.1.278 S-adenosyl-L-methionine + (indol-3-yl)acetate Arabidopsis thaliana
-
 S-adenosyl-L-homocysteine + methyl (indol-3-yl)acetate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.1.1.274 Clarkia breweri Q9SPV4
-
-
2.1.1.278 Arabidopsis thaliana Q9FLN8
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.1.1.274 N-terminal polyhistidine-tagged SAMT protein purified by Ni2+ affinity chromatography and gel filtration chromatography using a Superdex-75 column Clarkia breweri
2.1.1.278
-
 Arabidopsis thaliana

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.1.274 additional information no measurable methylation of jasmonic acid by wild-type SAMT using concentrations up to 5 mM Clarkia breweri ?
-
 ?
2.1.1.274 additional information wild-type is also able to methylate benzoic acid with 48% activity compared to salicylate methylation Clarkia breweri ?
-
 ?
2.1.1.274 S-adenosyl-L-methionine + 3-hydroxybenzoic acid 17% activity of wild-type enzyme compared to salicylate methylation Clarkia breweri S-adenosyl-L-homocysteine + methyl 3-hydroxybenzoate
-
 ?
2.1.1.274 S-adenosyl-L-methionine + jasmonic acid Y147S/M150H double mutant and Y147S/M150H/F347Y triple mutant are able to turn over jasmonic acid, while preserving substantial salicylate methylating activity Clarkia breweri S-adenosyl-L-homocysteine + methyl jasmonate
-
 ?
2.1.1.274 S-adenosyl-L-methionine + salicylate
-
 Clarkia breweri S-adenosyl-L-homocysteine + methyl salicylate
-
 ?
2.1.1.274 S-adenosyl-L-methionine + vanillic acid 5.1% activity of wild-type enzyme compared to salicylate methylation Clarkia breweri S-adenosyl-L-homocysteine + methyl 4-hydroxy-3-methoxybenzoate
-
 ?
2.1.1.278 S-adenosyl-L-methionine + (indol-3-yl)acetate
-
 Arabidopsis thaliana S-adenosyl-L-homocysteine + methyl (indol-3-yl)acetate
-
 ?

Subunits

EC Number Subunits Comment Organism
2.1.1.274 homodimer 2 * 41000 Clarkia breweri

Synonyms

EC Number Synonyms Comment Organism
2.1.1.274 SA carboxyl methyltransferase
-
 Clarkia breweri
2.1.1.274 SAMT
-
 Clarkia breweri
2.1.1.278 At5g55250
-
 Arabidopsis thaliana
2.1.1.278 IAA carboxylmethyltransferase
-
 Arabidopsis thaliana
2.1.1.278 IAMT
-
 Arabidopsis thaliana

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.1.1.274 0.092
-
 salicylate wild type enzyme, pH 7.5, 25°C Clarkia breweri
2.1.1.278 0.028
-
 (indol-3-yl)acetate pH 7.5, 25°C Arabidopsis thaliana

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
2.1.1.274 4
-
 salicylate wild type enzyme, pH 7.5, 25°C Clarkia breweri
2.1.1.278 2.15
-
 (indol-3-yl)acetate pH 7.5, 25°C Arabidopsis thaliana