Chlorophenol O-methyltransferase

In enzymology, a chlorophenol O-methyltransferase (EC 2.1.1.136) is an enzyme that catalyzes the chemical reaction

S-adenosyl-L-methionine + trichlorophenol S-adenosyl-L-homocysteine + trichloroanisole
chlorophenol O-methyltransferase
Identifiers
EC no.2.1.1.136
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

Thus, the two substrates of this enzyme are S-adenosyl methionine and trichlorophenol, whereas its two products are S-adenosylhomocysteine and trichloroanisole.

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:trichlorophenol O-methyltransferase. Other names in common use include halogenated phenol O-methyltransferase, trichlorophenol, and O-methyltransferase.

References

    • Kikuchi T, Oe T (1994). "Halogenated phenol O-methyltransferase, its production and deodorization using the same". Chem. Abstr. 127: 27468.


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