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Literature summary for 2.1.1.274 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)

Cloned (Comment) Organism
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

Protein Variants

Protein Variants Comment Organism
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
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)

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

Organism

Organism UniProt Comment Textmining
Populus trichocarpa A9PF83
-
-

Purification (Commentary)

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

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.95
-
below, recombinant wild-type PtSABATH4 with benzoic acid, pH 7.4, 25°C Populus trichocarpa
27.96
-
recombinant wild-type PtSABATH4 with salicylic acid, pH 7.4, 25°C Populus trichocarpa

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 ?
-
-
S-adenosyl-L-methionine + benzoate
-
Populus trichocarpa methyl benzoate + S-adenosyl-L-homocysteine
-
?
S-adenosyl-L-methionine + salicylate
-
Populus trichocarpa methyl salicylate + S-adenosyl-L-homocysteine
-
?

Synonyms

Synonyms Comment Organism
class II SABATH protein
-
Populus trichocarpa
More see also EC 2.1.1.273 Populus trichocarpa
PtSABATH4
-
Populus trichocarpa
S-adenosyl-L-methionine:salicylic acid carboxyl methyltransferase UniProt Populus trichocarpa
SABATH methyltransferase 4 UniProt Populus trichocarpa
SABATH4
-
Populus trichocarpa

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Populus trichocarpa

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
-
assay at Populus trichocarpa

Cofactor

Cofactor Comment Organism Structure
S-adenosyl-L-methionine
-
Populus trichocarpa

General Information

General Information Comment Organism
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
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
metabolism expression patterns of Populus SABATH genes under normal growth conditions and abiotic stress, overview Populus trichocarpa
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