Phosphatidyl-N-methylethanolamine N-methyltransferase

In enzymology, a phosphatidyl-N-methylethanolamine N-methyltransferase (EC 2.1.1.71) is an enzyme that catalyzes the chemical reaction

S-adenosyl-L-methionine + phosphatidyl-N-methylethanolamine S-adenosyl-L-homocysteine + phosphatidyl-N-dimethylethanolamine
phosphatidyl-N-methylethanolamine N-methyltransferase
Identifiers
EC no.2.1.1.71
CAS no.67167-73-1
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 phosphatidyl-N-methylethanolamine, whereas its two products are S-adenosylhomocysteine and phosphatidyl-N-dimethylethanolamine.

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:phosphatidyl-N-methylethanolamine N-methyltransferase. Other names in common use include phosphatidylmonomethylethanolamine methyltransferase, methyltransferase II, phospholipid methyltransferase, PLMT, phosphatidyl-N-methylethanolamine methyltransferase, phosphatidyl-N-monomethylethanolamine methyltransferase, phosphatidylethanolamine methyltransferase I, and phosphatidylmonomethylethanolamine methyltransferase. This enzyme participates in glycine, serine and threonine metabolism and glycerophospholipid metabolism.

References

    • Hirata F, Viveros OH, Diliberto EJ, Axelrod J (1978). "Identification and properties of two methyltransferases in conversion of phosphatidylethanolamine to phosphatidylcholine". Proc. Natl. Acad. Sci. U.S.A. 75 (4): 1718–21. doi:10.1073/pnas.75.4.1718. PMC 392410. PMID 25437.
    • Schneider WJ, Vance DE (1979). "Conversion of phosphatidylethanolamine to phosphatidylcholine in rat liver. Partial purification and characterization of the enzymatic activities". J. Biol. Chem. 254 (10): 3886–91. doi:10.1016/S0021-9258(18)50670-0. PMID 438165.


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