Biology:Phosphatidyl-N-methylethanolamine N-methyltransferase
| phosphatidyl-N-methylethanolamine N-methyltransferase | |||||||||
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| Identifiers | |||||||||
| EC number | 2.1.1.71 | ||||||||
| CAS number | 67167-73-1 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
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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 [math]\displaystyle{ \rightleftharpoons }[/math] S-adenosyl-L-homocysteine + phosphatidyl-N-dimethylethanolamine
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
- "Identification and properties of two methyltransferases in conversion of phosphatidylethanolamine to phosphatidylcholine". Proc. Natl. Acad. Sci. U.S.A. 75 (4): 1718–21. 1978. doi:10.1073/pnas.75.4.1718. PMID 25437.
- "Conversion of phosphatidylethanolamine to phosphatidylcholine in rat liver. Partial purification and characterization of the enzymatic activities". J. Biol. Chem. 254 (10): 3886–91. 1979. doi:10.1016/S0021-9258(18)50670-0. PMID 438165.
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