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2.1.1.68: caffeate O-methyltransferase

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

Word Map on EC 2.1.1.68

Reaction

S-adenosyl-L-methionine
+
3,4-dihydroxy-trans-cinnamate
=
S-adenosyl-L-homocysteine
+
3-methoxy-4-hydroxy-trans-cinnamate

Synonyms

3,4-dihydroxybenzaldehyde-O-methyltransferase, AtCOMT1, AtOMT1, benzenoid/phenylpropanoid meta/para-O-methyltransferase, Bmr12, Bradi3g16530, brown midrib 12, caffeate 3-O-methyltransferase, caffeate methyltransferase, caffeate/5-hydroxyferulate 3/5-O-methyltransferase, caffeic acid 3-O-methyltransferase, caffeic acid O-methyl-transferase, caffeic acid O-methyltransferase, caffeic acid O-methyltransferase 1, caffeic acid/5-hydroxyferulic acid 3/5-O-methyltransferase, caffeic O-methyl transferase, CCOMT, COMT, COMT-3D, COMT1, COMT2, COMT4, COMT6, DOMT, FGCOMT1, Lp OMT1, O-methyltransferase, O-methytransferase, OMT, OMT1, OMT3, OsCOMT1, RsOMT1, RsOMT3, S-adenosyl-L-methionine:caffeic acid-O-methyltransferase, Sb07g003860, Van OMT-2, Van OMT-3

ECTree

     2 Transferases
         2.1 Transferring one-carbon groups
             2.1.1 Methyltransferases
                2.1.1.68 caffeate O-methyltransferase

Crystallization

Crystallization on EC 2.1.1.68 - caffeate O-methyltransferase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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 COMT’s 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
-
crystallization from polyethylene glycol solution, 2.2 A resolution, complex with S-adenosyl-L-homocysteine and ferulic acid
crystallization from polyethylene glycol solution, 2.4 A resolution, complex with S-adenosyl-L-homocysteine and 5-hydroxyconiferaldehyde
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
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