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Literature summary extracted from

  • 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 (2018), Plant Cell Physiol., 59, 392-403 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.1.1.273 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) Populus trichocarpa
2.1.1.274 gene SABATH4, 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) Populus trichocarpa
2.1.1.278 gene SABATH1, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, overview, recombinant expression of soluble His-tagged enzyme in Escherichia coli strain BL21(DE3) Populus trichocarpa

Protein Variants

EC Number Protein Variants Comment Organism
2.1.1.273 H157M site-directed mutagenesis, this mutation results in a switch from a preference for benzoic acid (BA) over salicylic acid (SA) in wild-type PtSABATH24 to a preference for SA over BA in the H157M mutant Populus trichocarpa
2.1.1.274 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 Populus trichocarpa
2.1.1.274 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 Populus trichocarpa

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.1.1.273 S-adenosyl-L-methionine + benzoate Populus trichocarpa
-
 methyl benzoate + S-adenosyl-L-homocysteine
-
 ?
2.1.1.273 S-adenosyl-L-methionine + salicylate Populus trichocarpa
-
 methyl salicylate + S-adenosyl-L-homocysteine
-
 ?
2.1.1.274 S-adenosyl-L-methionine + benzoate Populus trichocarpa
-
 methyl benzoate + S-adenosyl-L-homocysteine
-
 ?
2.1.1.274 S-adenosyl-L-methionine + salicylate Populus trichocarpa
-
 methyl salicylate + S-adenosyl-L-homocysteine
-
 ?
2.1.1.278 S-adenosyl-L-methionine + indole-3-acetate Populus trichocarpa
-
 methyl indole-3-acetate + S-adenosyl-L-homocysteine
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.1.1.273 Populus trichocarpa B9IPD3
-
-
2.1.1.274 Populus trichocarpa A9PF83
-
-
2.1.1.278 Populus trichocarpa B9GJG7
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.1.1.273 recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography Populus trichocarpa
2.1.1.274 recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography Populus trichocarpa
2.1.1.278 recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography Populus trichocarpa

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.1.1.278 bud
-
 Populus trichocarpa
-
2.1.1.278 leaf
-
 Populus trichocarpa
-
2.1.1.278 additional information gene PtSABATH1 is expressed in the root, shoot, leaf and bud tissues, but not expressed in the Populus flower Populus trichocarpa
-
2.1.1.278 root
-
 Populus trichocarpa
-
2.1.1.278 shoot
-
 Populus trichocarpa
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.1.1.273 56.97
-
 recombinant wild-type PtSABATH24 with benzoic acid, pH 7.4, 25°C Populus trichocarpa
2.1.1.274 2.95
-
 below, recombinant wild-type PtSABATH4 with benzoic acid, pH 7.4, 25°C Populus trichocarpa
2.1.1.274 27.96
-
 recombinant wild-type PtSABATH4 with salicylic acid, pH 7.4, 25°C Populus trichocarpa
2.1.1.278 8.98
-
 recombinant wild-type PtSABATH4 with farnesoic acid, pH 7.4, 25°C Populus trichocarpa
2.1.1.278 66.51
-
 recombinant wild-type PtSABATH1 with indole-3-acetate, pH 7.4, 25°C Populus trichocarpa

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.1.273 additional information 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 Populus trichocarpa ?
-
-
2.1.1.273 S-adenosyl-L-methionine + benzoate
-
 Populus trichocarpa methyl benzoate + S-adenosyl-L-homocysteine
-
 ?
2.1.1.273 S-adenosyl-L-methionine + salicylate
-
 Populus trichocarpa methyl salicylate + S-adenosyl-L-homocysteine
-
 ?
2.1.1.274 additional information 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 S-adenosyl-L-methionine + benzoate
-
 Populus trichocarpa methyl benzoate + S-adenosyl-L-homocysteine
-
 ?
2.1.1.274 S-adenosyl-L-methionine + salicylate
-
 Populus trichocarpa methyl salicylate + S-adenosyl-L-homocysteine
-
 ?
2.1.1.278 additional information PtSABATH1, also named PtIAMT1, can catalyze the formation of methyl indole-3-acetate (MeIAA) using SAM as a methyl donor and indole-3-acetic acid (IAA) as a methyl acceptor. Enzyme PtSABATH1 does not show any activity towards substrates benzoic acid, jasmonic acid, salicylic acid, vanillic acid, nicotinic acid, coumalic acid, or trans-cinnamic acid. Compared with other Populus SABATH proteins (PtSABATH2, 3, 12, 17, 21 and 24 have very weak activities towards IAA), PtSABATH1 shows at least 40.5fold higher activity towards IAA Populus trichocarpa ?
-
-
2.1.1.278 S-adenosyl-L-methionine + farnesoate low activity Populus trichocarpa methyl farnesoate + S-adenosyl-L-homocysteine
-
 ?
2.1.1.278 S-adenosyl-L-methionine + indole-3-acetate
-
 Populus trichocarpa methyl indole-3-acetate + S-adenosyl-L-homocysteine
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.1.1.273 class II SABATH protein
-
 Populus trichocarpa
2.1.1.273 More see also EC 2.1.1.274 Populus trichocarpa
2.1.1.273 PtSABATH24
-
 Populus trichocarpa
2.1.1.273 S-adenosyl-L-methionine:salicylic acid carboxyl methyltransferase UniProt Populus trichocarpa
2.1.1.273 SABATH methyltransferase 4 UniProt Populus trichocarpa
2.1.1.273 SABATH24
-
 Populus trichocarpa
2.1.1.274 class II SABATH protein
-
 Populus trichocarpa
2.1.1.274 More see also EC 2.1.1.273 Populus trichocarpa
2.1.1.274 PtSABATH4
-
 Populus trichocarpa
2.1.1.274 S-adenosyl-L-methionine:salicylic acid carboxyl methyltransferase UniProt Populus trichocarpa
2.1.1.274 SABATH methyltransferase 4 UniProt Populus trichocarpa
2.1.1.274 SABATH4
-
 Populus trichocarpa
2.1.1.278 class I SABATH protein
-
 Populus trichocarpa
2.1.1.278 PtIAMT1
-
 Populus trichocarpa
2.1.1.278 PtSABATH1
-
 Populus trichocarpa
2.1.1.278 S-adenosyl-L-methionine:salicylic acid carboxyl methyltransferase UniProt Populus trichocarpa
2.1.1.278 SABATH methyltransferase 1 UniProt Populus trichocarpa
2.1.1.278 SABATH1
-
 Populus trichocarpa

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.1.1.273 25
-
 assay at Populus trichocarpa
2.1.1.274 25
-
 assay at Populus trichocarpa
2.1.1.278 25
-
 assay at Populus trichocarpa

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.1.1.273 7.4
-
 assay at Populus trichocarpa
2.1.1.274 7.4
-
 assay at Populus trichocarpa
2.1.1.278 7.4
-
 assay at Populus trichocarpa

Cofactor

EC Number Cofactor Comment Organism Structure
2.1.1.273 S-adenosyl-L-methionine
-
 Populus trichocarpa
2.1.1.274 S-adenosyl-L-methionine
-
 Populus trichocarpa
2.1.1.278 S-adenosyl-L-methionine
-
 Populus trichocarpa

General Information

EC Number General Information Comment Organism
2.1.1.273 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 Populus trichocarpa
2.1.1.273 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 Populus trichocarpa
2.1.1.273 metabolism expression patterns of Populus SABATH genes under normal growth conditions and abiotic stress, overview Populus trichocarpa
2.1.1.274 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 Populus trichocarpa
2.1.1.274 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. 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. The mutation of His157 of PtSABATH24 (EC 2.1.1.273) 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 PtSABATH4 mutation M314V results in decreased enzymatic activities towards both the substrates salicylic acid (SA) over benzoic acid (BA), but not in a substrate switch Populus trichocarpa
2.1.1.274 metabolism expression patterns of Populus SABATH genes under normal growth conditions and abiotic stress, overview Populus trichocarpa
2.1.1.274 additional information three-dimensional structure modeling of PtSABATH4 based on the 1M6E crystal structure. Similar to 1M6E, residues Met156 and Met314 of PtSABATH4 also create a molecular clamp that encompasses the benzyl ring of salicylate Populus trichocarpa
2.1.1.278 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. Populus class I SABATH gene (PtSABATH1) is grouped into clade I, Populus contains only one class I SABATH gene (PtSABATH1) Populus trichocarpa
2.1.1.278 metabolism expression patterns of Populus SABATH genes under normal growth conditions and abiotic stress, overview Populus trichocarpa
2.1.1.278 physiological function of Populus SABATH enzymes, only PtSABATH1 has high activity towards indole-3-acetic acid (IAA), and can convert IAA to methyl-IAA, indicating that PtSABATH1 might play an important role in auxin homeostasis Populus trichocarpa