Biology:Caffeate O-methyltransferase

From HandWiki
Short description: Enzyme


Caffeate O-methyltransferase
Alfalfa COMT dimer with bound substrates. PDB: 1KYW
Identifiers
EC number2.1.1.68
CAS number50936-45-3
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO

Caffeate O-methyltransferase (EC 2.1.1.68) is an enzyme that catalyzes the chemical reaction

  1. REDIRECT Template:Chemical reaction

This is a methylation reaction in which caffeic acid is converted to ferulic acid. The methyl group comes from the cofactor, S-adenosyl methionine (SAM), which becomes S-adenosyl-L-homocysteine (SAH).[1][2][3]

The 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.[4]

Structural studies

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

References

  1. "Evidence for the formation of methoxyl groups of ferulic and sinapic acid in Bambusa by the same O-methyltransferase". Phytochemistry 12 (12): 2873–2875. 1973. doi:10.1016/0031-9422(73)80498-4. Bibcode1973PChem..12.2873S. 
  2. Hahlbrock K; Schaller-Hekeler, B; Knobloch, KH; Wellman, E; Grisebach, H; Hahlbrock, K (1974). "Coordinated changes in enzyme activities of phenylpropanoid metabolism during the growth of soybean cell suspension cultures". Biochim. Biophys. Acta 362 (3): 417–24. doi:10.1016/0304-4165(74)90137-8. PMID 4472044. 
  3. "Purification and properties of S-adenosyl-L-methionine: caffeic acid O-methyltransferase from leaves of spinach beet (Beta vulgaris L)". Biochim. Biophys. Acta 403 (2): 301–14. 1975. doi:10.1016/0005-2744(75)90060-1. PMID 241400. 
  4. Enzyme 2.1.1.68 at KEGG Pathway Database.