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2.1.1.278: indole-3-acetate O-methyltransferase

This is an abbreviated version!
For detailed information about indole-3-acetate O-methyltransferase, go to the full flat file.

Word Map on EC 2.1.1.278

Reaction

S-adenosyl-L-methionine
+
(indol-3-yl)acetate
=
S-adenosyl-L-homocysteine
 +
methyl (indol-3-yl)acetate

Synonyms

At5g55250, AtIAMT1, class I SABATH protein, IAA carboxyl methyltransferase, IAA carboxylmethyltransferase, IAA methyltransferase, IAA methyltransferase1, IAA-methyltransferase-1, IAMT, IAMT1, indole-3-acetic acid carboxyl methyltransferase, indole-3-acetic acid methyltransferase, indole-3-acetic acid-methyltransferase-1, OsIAMT1, OsSABATH4, PaIAMT, PaSABATH1, PtIAMT1, PtSABATH1, S-adenosyl-L-methionine:salicylic acid carboxyl methyltransferase, SABATH methyltransferase 1, SABATH1

ECTree

     2 Transferases
         2.1 Transferring one-carbon groups
             2.1.1 Methyltransferases
                2.1.1.278 indole-3-acetate O-methyltransferase

General Information

General Information on EC 2.1.1.278 - indole-3-acetate O-methyltransferase

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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
overexpression of IAMT1 causes a decrease in auxin signalling. Reduction of indole-3-acetic acid methyltransferase activity compensates for high-temperature male sterility in Arabidopsis thaliana. Attenuation of IAMT1 activity promotes fertilization and enhances thermotolerance. The iamt1 mutant shows increased auxin signalling in funiculi, which correlated with a higher growth rate of wild-type pollen in contact with mutant ovaries and premature ovule fertilization. While the production of seeds per fruit is similar in the wild-type and the mutant at 20°C, exposure to 29°C causes a more severe decrease in fertility in the wild-type than in the mutant. Loss of IAMT1 activity is also associated with the production of more nodes after flowering and higher tolerance of the shoot apical meristem to higher temperatures. As a consequence, the productivity of the iamt1 mutant under higher temperatures is more than double of that of the wild-type, with almost no apparent trade-off
metabolism
expression patterns of Populus SABATH genes under normal growth conditions and abiotic stress, overview
physiological function
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