ID: | 2.1.1.129 |
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Description: | Inositol 4-methyltransferase. |
Alternative Name: |
S-adenosyl-L-methionine:myo-inositol 4-O-methyltransferase. Myo-inositol 6-O-methyltransferase. Myo-inositol 4-O-methyltransferase. |
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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 2.1.1.129 |
BRENDA Enzyme Link: | BRENDA 2.1.1.129 |
KEGG Enzyme Link: | KEGG2.1.1.129 |
BioCyc Enzyme Link: | BioCyc 2.1.1.129 |
ExPASy Enzyme Link: | ExPASy2.1.1.129 |
EC2PDB Enzyme Link: | EC2PDB 2.1.1.129 |
ExplorEnz Enzyme Link: | ExplorEnz 2.1.1.129 |
PRIAM enzyme-specific profiles Link: | PRIAM 2.1.1.129 |
IntEnz Enzyme Link: | IntEnz 2.1.1.129 |
MEDLINE Enzyme Link: | MEDLINE 2.1.1.129 |
MSA: | |
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Phylogenetic Tree: | |
Uniprot: | |
M-CSA: |
RHEA:23248 | myo-inositol + S-adenosyl-L-methionine = 1D-4-O-methyl-myo-inositol + H(+) + 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 |
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Characterization of IMT1, myo-inositol O-methyltransferase, from Mesembryanthemum crystallinum. | Rammesmayer G, Pichorner H, Adams P, Jensen RG, Bohnert HJ | 1995 Sep 10 | 7574673 |
A novel methyl transferase induced by osmotic stress in the facultative halophyte Mesembryanthemum crystallinum. | Vernon DM, Bohnert HJ | 1992 Jun | 1600940 |