ID: | 2.1.1.278 |
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Description: | Indole-3-acetate O-methyltransferase. |
Alternative Name: |
IAA carboxylmethyltransferase. |
Cath: | 1.10.1200.220; 3.40.50.150; |
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Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.UniProtKB Enzyme Link: | UniProtKB 2.1.1.278 |
BRENDA Enzyme Link: | BRENDA 2.1.1.278 |
KEGG Enzyme Link: | KEGG2.1.1.278 |
BioCyc Enzyme Link: | BioCyc 2.1.1.278 |
ExPASy Enzyme Link: | ExPASy2.1.1.278 |
EC2PDB Enzyme Link: | EC2PDB 2.1.1.278 |
ExplorEnz Enzyme Link: | ExplorEnz 2.1.1.278 |
PRIAM enzyme-specific profiles Link: | PRIAM 2.1.1.278 |
IntEnz Enzyme Link: | IntEnz 2.1.1.278 |
MEDLINE Enzyme Link: | MEDLINE 2.1.1.278 |
MSA: | |
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Phylogenetic Tree: | |
Uniprot: | |
M-CSA: |
RHEA:36131 | (indol-3-yl)acetate + S-adenosyl-L-methionine = methyl (indol-3-yl)acetate + S-adenosyl-L-homocysteine |
RULE(radius=1) | [*:1]-[OH;+0:2].[*:3]-[S+;H0:4](-[*:5])-[CH3;+0:6]>>[*:1]-[O;H0;+0:2]-[CH3;+0:6].[*:3]-[S;H0;+0:4]-[*:5] |
Reaction | ![]() |
Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
Title | Authors | Date | PubMed ID |
---|---|---|---|
Structural, biochemical, and phylogenetic analyses suggest that indole-3-acetic acid methyltransferase is an evolutionarily ancient member of the SABATH family. | Zhao N, Ferrer JL, Ross J, Guan J, Yang Y, Pichersky E, Noel JP, Chen F | 2008 Feb | 18162595 |
The possible action mechanisms of indole-3-acetic acid methyl ester in Arabidopsis. | Li L, Hou X, Tsuge T, Ding M, Aoyama T, Oka A, Gu H, Zhao Y, Qu LJ | 2008 Mar | 17926040 |
Methyl-3-indolylacetate inhibits cancer cell invasion by targeting the MEK1/2-ERK1/2 signaling pathway. | Zhang S, Li Z, Wu X, Huang Q, Shen HM, Ong CN | 2006 Dec | 17172432 |
Structural basis for substrate recognition in the salicylic acid carboxyl methyltransferase family. | Zubieta C, Ross JR, Koscheski P, Yang Y, Pichersky E, Noel JP | 2003 Aug | 12897246 |