Literature summary for 2.1.1.278 extracted from

Chaiprasongsuk, M.; Zhang, C.; Qian, P.; Chen, X.; Li, G.; Trigiano, R.N.; Guo, H.; Chen, F.
Biochemical characterization in Norway spruce (Picea abies) of SABATH methyltransferases that methylate phytohormones (2018), Phytochemistry, 149, 146-154 .

Search for more literature for 2.1.1.278

Cloned(Commentary)

Cloned (Comment)	Organism
gene PaSABATH1, DNA and amino acid sequence determination and analysis, sequence comparisons, genetic organization and localization of SABATH genes in the genome of Picea abies, overview. Sequence similarities among PaSABATHs range from 49% to 91%. Most PaSABATH genes have three introns with the exception of PaSABATH4, PaSABATH5 and PaSABATH10, each of which contains two introns. Phylogenetic analysis and tree	Picea abies

Cloned (Comment)

Organism

gene PaSABATH1, DNA and amino acid sequence determination and analysis, sequence comparisons, genetic organization and localization of SABATH genes in the genome of Picea abies, overview. Sequence similarities among PaSABATHs range from 49% to 91%. Most PaSABATH genes have three introns with the exception of PaSABATH4, PaSABATH5 and PaSABATH10, each of which contains two introns. Phylogenetic analysis and tree

Picea abies

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
S-adenosyl-L-methionine + indole-3-acetic acid	Picea abies	-	S-adenosyl-L-homocysteine + methyl indole-3-acetic acid	-	?

Organism

Organism	UniProt	Comment	Textmining
Picea abies	-	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
cone	-	Picea abies	-
additional information	mixed tissues including needles, stems, and young male cones and female cones are collected from a mature Norway spruce (Picea abies) tree grown on the campus of the University of Tennessee, Knoxville, TN with a GPS coordinates of 35.948 and -83.942	Picea abies	-
needle	-	Picea abies	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	PaSABATH1 has the highest level of specific activity with IAA and is renamed as PaIAMT. No activity with salicylic acid, jasmonic acid, and giberellic acid 3	Picea abies	?	-	-
S-adenosyl-L-methionine + indole-3-acetic acid	-	Picea abies	S-adenosyl-L-homocysteine + methyl indole-3-acetic acid	-	?

Synonyms

Synonyms	Comment	Organism
IAA methyltransferase	-	Picea abies
PaIAMT	-	Picea abies
PaSABATH1	-	Picea abies

Cofactor

Cofactor	Comment	Organism	Structure
S-adenosyl-L-methionine	-	Picea abies

General Information

General Information	Comment	Organism
evolution	the enzyme belongs to the protein family of SABATH methyltransferases, ten genes encode isozymes PaSABATH1-10. Five of the PaSABATH isozymes (PaSABATH3, PaSABATH6, PaSABATH7, PaSABATH8, and PaSABATH9) do not show activity with any of the four substrates, i.e. indole-3-acetic acid, jasmonic acid, giberellic acid A3, and salicylic acid, the other five of the PaSABATHs each show activity with one or more of the four substrates. PaSABATH1 has the highest level of specific activity with indole-3-acetic acid and is renamed as PaIAMT (EC 2.1.1.278). 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. PaSABATH4, PaSABATH5 and PaSABATH10 show the highest level of specific activity with jasmonic acid and are renamed PaJAMT1, PaJAMT2, and PaJAMT3, respectively (EC 2.1.1.141). Their products are confirmed to be methyljasmonate	Picea abies
additional information	a structural model for PaIAMTis generated to understand the origin of substrate specificity of PaSABATH methyltransferase. The active site of the PaIAMT model is superposed with that of the X-ray structure of IAMT (PDB ID 3B5I). The substrate indole-3-acetic acid (IAA) is docked into the active site in such way that its carboxyl moiety is located at a suitable position for accepting the methyl group from SAM (AdoMet). The active site of the enzymes is able to accommodate IAA in a reactive configuration. The enzyme has relatively high specificity for IAA. This is in contrast to docking jasmonate (JA) into the active site. When JA is docked into the active sites with the carboxyl moiety located at the suitable position for accepting the methyl group, the side chain of JA made steric clashes with some of the active site residues (F267 and L266 from PaIAMT), and the active site is therefore not able to accommodate JA for the methyl transfer	Picea abies