EC Number   |
|---|
    2.1.1.68 | - |
| 2.1.1.68 | apo-form and binary complex with S-adenosyl-methionine, to 2.1 and 2.8 A resolution, respectively, and molecular modeling of the ternary complex structure with 5-hydroxyconiferaldehyde |
| 2.1.1.68 | crystallization from polyethylene glycol solution, 2.2 A resolution, complex with S-adenosyl-L-homocysteine and ferulic acid |
| 2.1.1.68 | crystallization from polyethylene glycol solution, 2.4 A resolution, complex with S-adenosyl-L-homocysteine and 5-hydroxyconiferaldehyde |
| 2.1.1.68 | molecular docking of 16 putative substrates (intermediates of monolignol biosynthesis pathway). Both caffeic acid-O-methyltransferase and caffeoyl-coenzyme A-O-methyltransferase, EC 2.1.1.104, interact with all 16 substrates in a similar manner, with thiol esters being the most potent and binding of these putative substrates to caffeoyl-coenzyme A-O-methyltransferase being more efficient |
| 2.1.1.68 | x-ray crystallographic structures of Lp OMT1 are reported in open conformational state, apo- and holoenzyme forms and, most significantly, in a closed conformational state complexed with the products S-adenosyl-L-homocysteine and sinapaldehyde. The product-bound complex reveals the postmethyl-transfer organization of COMTs catalytic groups with reactant molecules and the fully formed phenolic-ligand binding site. The core scaffold of the phenolic ligand forges a hydrogen-bonding network involving the 4-hydroxy group that anchors the aromatic ring and thereby permits only metahydroxyl groups to be positioned for transmethylation |
