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Literature summary for 2.1.1.68 extracted from

  • Louie, G.V.; Bowman, M.E.; Tu, Y.; Mouradov, A.; Spangenberg, G.; Noel, J.P.
    Structure-function analyses of a caffeic acid O-methyltransferase from perennial ryegrass reveal the molecular basis for substrate preference (2010), Plant Cell, 22, 4114-4127.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
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 Lolium perenne

Organism

Organism UniProt Comment Textmining
Lolium perenne
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
S-adenosyl-L-methionine + 5-hydroxyconiferaldehyde
-
Lolium perenne ?
-
?
S-adenosyl-L-methionine + 5-hydroxyferulic acid
-
Lolium perenne S-adenosyl-L-homocysteine + sinapic acid
-
?
S-adenosyl-L-methionine + caffeic acid
-
Lolium perenne ?
-
?
S-adenosyl-L-methionine + caffeoyl alcohol
-
Lolium perenne ?
-
?
S-adenosyl-L-methionine + caffeoyl aldehyde
-
Lolium perenne ?
-
?

Synonyms

Synonyms Comment Organism
Lp OMT1
-
Lolium perenne

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
22
-
assay at Lolium perenne

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
assay at Lolium perenne