| alkylglycerol monooxygenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.14.16.5 | ||||||||
| CAS no. | 37256-82-9 | ||||||||
| 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 | ||||||||
| |||||||||
Alkylglycerol monooxygenase (AGMO) (EC 1.14.16.5) is an enzyme that catalyzes the hydroxylation of alkylglycerols, a specific subclass of ether lipids. This enzyme was first described in 1964 as a pteridine-dependent ether lipid cleaving enzyme.[1] In 2010 finally, the gene coding for alkylglycerol monooxygenase was discovered as transmembrane protein 195 (TMEM195) on chromosome 7.[2] In analogy to the enzymes phenylalanine hydroxylase, tyrosine hydroxylase, tryptophan hydroxylase and nitric oxide synthase, alkylglycerol monooxygenase critically depends on the cofactor tetrahydrobiopterin and iron.
The reaction catalyzed by alkylglycerol monooxygenase:
- 1-alkyl-sn-glycerol + tetrahydrobiopterin + O2 1-hydroxyalkyl-sn-glycerol + 6,7[8H]-dihydrobiopterin + H2O
The unstable intermediate product 1-hydroxyalkyl-sn-glycerol rearranges into the fatty aldehyde and the free glycerol derivative. The fatty aldehyde is then further oxidized to the corresponding acid by fatty aldehyde dehydrogenase.
Alkylglycerol monooxygenase is a membrane-bound mixed-function oxidase and harbours a fatty acid hydroxylase motif. The iron is believed to be coordinated by a diiron center composed of eight histidines, which can be found in all enzymes containing this motif.
Nomenclature
The systematic name for this enzyme is 1-alkyl-sn-glycerol,tetrahydrobiopterin:oxygen oxidoreductase. Other names in use are glyceryl-ether monooxygenase, glyceryl-ether cleaving enzyme, glyceryl ether oxygenase, glyceryl etherase, and O-alkylglycerol monooxygenase.
References
- ^ Tietz, AA; Lindberg, M; Kennedy, EP (December 1964). "A New Pteridine-Requiring Enzyme System For The Oxidation Of Glyceryl Ethers". The Journal of Biological Chemistry. 239 (12): 4081–90. doi:10.1016/S0021-9258(18)91137-3. PMID 14247652.
- ^ Watschinger, K (2010). "Identification of the gene encoding alkylglycerol monooxygenase defines a third class of tetrahydrobiopterin-dependent enzymes". Proc. Natl. Acad. Sci. U.S.A. 107 (31): 13672–13677. Bibcode:2010PNAS..10713672W. doi:10.1073/pnas.1002404107. PMC 2922233. PMID 20643956.
Further reading
- Watschinger K, Keller MA, Hermetter A, Golderer G, Werner-Felmayer G, Werner ER (2009). "Glyceryl ether monooxygenase resembles aromatic amino acid hydroxylases in metal ion and tetrahydrobiopterin dependence". Biol. Chem. 390 (1): 3–10. doi:10.1515/BC.2009.010. PMC 2847825. PMID 19007315.
- Werner ER, Hermetter A, Prast H, Golderer G, Werner-Felmayer G (2007). "Widespread occurrence of glyceryl ether monooxygenase activity in rat tissues detected by a novel assay". J. Lipid Res. 48 (6): 1422–1427. doi:10.1194/jlr.D600042-JLR200. PMC 2851153. PMID 17303893.
- Ishibashi T, Imai Y (1983). "Solubilization and partial characterization of alkylglycerol monooxygenase from rat liver microsomes". Eur. J. Biochem. 132 (1): 23–7. doi:10.1111/j.1432-1033.1983.tb07320.x. PMID 6840084.
- Pfleger RC, Piantadosi C, Snyder F (1967). "The biocleavage of isomeric glyceryl ethers by soluble liver enzymes in a variety of species". Biochim. Biophys. Acta. 144 (3): 633–48. doi:10.1016/0005-2760(67)90052-5. PMID 4383918.
- Snyder F, Malone B, Piantadosi C (1973). "Tetrahydropteridine-dependent cleavage enzyme for O-alkyl lipids: substrate specificity". Biochim. Biophys. Acta. 316 (2): 259–65. doi:10.1016/0005-2760(73)90018-0. PMID 4355017.
- Soodsma JF, Piantadosi C, Snyder F (1972). "Partial characterization of the alkylglycerol cleavage enzyme system of rat liver". J. Biol. Chem. 247 (12): 3923–9. doi:10.1016/S0021-9258(19)45123-5. PMID 4402391.
This page was last edited on 11 December 2023, at 01:44