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Alkylglycerol monooxygenase

Class of enzymes


Summary

Class of enzymes

FieldValue
Namealkylglycerol monooxygenase
EC_number1.14.16.5
CAS_number37256-82-9
GO_code0050479

Alkylglycerol monooxygenase (AGMO) () 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. In 2010 finally, the gene coding for alkylglycerol monooxygenase was discovered as transmembrane protein 195 (TMEM195) on chromosome 7. 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 \rightleftharpoons 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

References

  1. Tietz, AA. (December 1964). "A New Pteridine-Requiring Enzyme System For The Oxidation Of Glyceryl Ethers.". The Journal of Biological Chemistry.
  2. 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..
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