Caffeate O-methyltransferase

{{infobox enzyme

| Name = caffeate O-methyltransferase

| EC_number = 2.1.1.68

| CAS_number = 50936-45-3

| GO_code = 0047763

| image =Alfalfa caffeate O-methyltransferase PDB 1KYW.png

| width =

| caption =Alfalfa COMT dimer with bound substrates. {{PDB|1KYW}}

|name=Caffeic acid 3-O-methyltransferase}}

In enzymology, a caffeate O-methyltransferase ({{EC number|2.1.1.68}}) is an enzyme that catalyzes the chemical reaction

:SAM + caffeic acid $\rightleftharpoons$ SAH + ferulic acid

Thus, the two substrates of this enzyme are S-adenosyl methionine and 3,4-dihydroxy-trans-cinnamate (caffeic acid), whereas its two products are S-adenosylhomocysteine and 3-methoxy-4-hydroxy-trans-cinnamate (ferulic acid).

This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:3,4-dihydroxy-trans-cinnamate 3-O-methyltransferase. Other names in common use include caffeate methyltransferase, caffeate 3-O-methyltransferase, and S-adenosyl-L-methionine:caffeic acid-O-methyltransferase. This enzyme participates in phenylpropanoid biosynthesis.

Structural studies

As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes {{PDB link|1KYW}} and {{PDB link|1KYZ}}.

References

{{cite journal | author = Hahlbrock K | date = 1974 | title = Coordinated changes in enzyme activities of phenylpropanoid metabolism during the growth of soybean cell suspension cultures | journal = Biochim. Biophys. Acta | volume = 362 | pages = 417–24 | pmid = 4472044 | last2 = Schaller-Hekeler | first2 = B | last3 = Knobloch | first3 = KH | last4 = Wellman | first4 = E | last5 = Grisebach | first5 = H | last6 = Hahlbrock | first6 = K | issue = 3 | doi=10.1016/0304-4165(74)90137-8}}
{{cite journal |vauthors=Poulton JE, Butt VS | date = 1975 | title = Purification and properties of S-adenosyl-L-methionine: caffeic acid O-methyltransferase from leaves of spinach beet (Beta vulgaris L) | journal = Biochim. Biophys. Acta | volume = 403 | pages = 301–14 | pmid = 241400 | issue = 2 | doi=10.1016/0005-2744(75)90060-1}}
{{cite journal |vauthors=Shimada M, Kuroda H, Higuchi T | date = 1973 | title = Evidence for the formation of methoxyl groups of ferulic and sinapic acid in Bambusa by the same O-methyltransferase | journal = Phytochemistry | volume = 12 | pages = 2873–2875 | doi = 10.1016/0031-9422(73)80498-4 | issue = 12 | bibcode = 1973PChem..12.2873S }}

Category:EC 2.1.1

Category:Enzymes of known structure

Category:O-methylated hydroxycinnamic acids metabolism