| plasmanylethanolamine desaturase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.14.99.19 | ||||||||
| CAS no. | 39391-13-4 | ||||||||
| 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 | ||||||||
| |||||||||
In enzymology, a plasmanylethanolamine desaturase (EC 1.14.99.19) is an enzyme that catalyzes the chemical reaction
- O-1-alkyl-2-acyl-sn-glycero-3-phosphoethanolamine + AH2 + O2 O-1-alk-1-enyl-2-acyl-sn-glycero-3-phosphoethanolamine + A + 2 H2O
The 3 substrates of this enzyme are O-1-alkyl-2-acyl-sn-glycero-3-phosphoethanolamine, an electron acceptor AH2, and O2, whereas its 3 products are O-1-alk-1-enyl-2-acyl-sn-glycero-3-phosphoethanolamine, the reduction product A, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derive from O miscellaneous. The systematic name of this enzyme class is O-1-alkyl-2-acyl-sn-glycero-3-phosphoethanolamine,hydrogen-donor:oxy gen oxidoreductase. Other names in common use include alkylacylglycerophosphoethanolamine desaturase, alkylacylglycero-phosphorylethanolamine dehydrogenase, dehydrogenase, alkyl-acylglycerophosphorylethanolamine, 1-O-alkyl-2-acyl-sn-glycero-3-phosphorylethanolamine desaturase, and 1-O-alkyl 2-acyl-sn-glycero-3-phosphorylethanolamine desaturase. This enzyme participates in ether lipid metabolism. It requires NADPH.
Plasmanylethanolamine desaturase used to be described as an orphan enzyme, that is one whose activity is known but whose identity (gene, protein sequence) is unknown. It has now been identified and corresponds to protein CarF in bacteria and TMEM189 in humans (and animals). It contains the pfam10520 lipid desaturase domain which has 8 conserved histidines and which is also found in FAD4 plant desaturases. Mice lacking plasmanylethanolamine desaturase lack plasmalogens in their tissues and have reduced body weight.
References
- Werner, Ernst R.; Keller, Markus A.; Sailer, Sabrina; Lackner, Katharina; Koch, Jakob; Hermann, Martin; Coassin, Stefan; Golderer, Georg; Werner-Felmayer, Gabriele; Zoeller, Raphael A.; Hulo, Nicolas (April 2020). "The TMEM189 gene encodes plasmanylethanolamine desaturase which introduces the characteristic vinyl ether double bond into plasmalogens". Proceedings of the National Academy of Sciences of the United States of America. 117 (14): 7792–7798. doi:10.1073/pnas.1917461117. ISSN 1091-6490. PMC 7149458. PMID 32209662.
- Gallego-García A, Monera-Girona AJ, Pajares-Martínez E, Bastida-Martínez E, Pérez-Castaño R, Iniesta AA, Fontes M, Padmanabhan S, Elías-Arnanz M (October 2019). "A bacterial light response reveals an orphan desaturase for human plasmalogen synthesis". Science. 366 (6461): 128–132. Bibcode:2019Sci...366..128G. doi:10.1126/science.aay1436. PMID 31604315.
- Werner, Ernst R.; Keller, Markus A.; Sailer, Sabrina; Seppi, Daniele; Golderer, Georg; Werner-Felmayer, Gabriele; Zoeller, Raphael A.; Watschinger, Katrin (May 2018). "A novel assay for the introduction of the vinyl ether double bond into plasmalogens using pyrene-labeled substrates". Journal of Lipid Research. 59 (5): 901–909. doi:10.1194/jlr.D080283. ISSN 1539-7262. PMC 5928432. PMID 29540573.
- Paltauf F, Holasek A (March 1973). "Enzymatic synthesis of plasmalogens. Characterization of the 1-O-alkyl-2-acyl-8n-glycero-3-phosphorylethanolamine desaturase from mucosa of hamster small intestine". The Journal of Biological Chemistry. 248 (5): 1609–15. doi:10.1016/S0021-9258(19)44234-8. PMID 4144394.
- Wykle RL, Blank ML, Malone B, Snyder F (September 1972). "Evidence for a mixed function oxidase in the biosynthesis of ethanolamine plasmalogens from 1-alkyl-2-acyl-sn-glycero-3-phosphorylethanolamine". The Journal of Biological Chemistry. 247 (17): 5442–7. doi:10.1016/S0021-9258(20)81125-9. PMID 4403444.