Caffeate O-methyltransferase

From Wikipedia, the free encyclopedia

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

S-adenosyl-L-methionine + 3,4-dihydroxy-trans-cinnamate $\rightleftharpoons$ S-adenosyl-L-homocysteine + 3-methoxy-4-hydroxy-trans-cinnamate

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

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.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] Structural studies

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

[edit] References

IUBMB entry for 2.1.1.68
BRENDA references for 2.1.1.68 (Recommended.)
PubMed references for 2.1.1.68
PubMed Central references for 2.1.1.68
Google Scholar references for 2.1.1.68
Hahlbrock K (1974). "Coordinated changes in enzyme activities of phenylpropanoid metabolism during the growth of soybean cell suspension cultures". Biochim. Biophys. Acta. 362: 417–24. PMID 4472044.
Poulton JE, Butt VS (1975). "Purification and properties of S-adenosyl-L-methionine: caffeic acid O-methyltransferase from leaves of spinach beet (Beta vulgaris L)". Biochim. Biophys. Acta. 403: 301–14. PMID 241400.
Shimada M, Kuroda H and Higuchi T (1973). "Evidence for the formation of methoxyl groups of ferulic and sinapic acid in Bambusa by the same O-methyltransferase". Phytochemistry 12: 2873–2875. doi:10.1016/0031-9422(73)80498-4.