Enzymes
UniProtKB help_outline | 1,825 proteins |
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- Name help_outline (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin Identifier CHEBI:59560 (Beilstein: 4699705; CAS: 17528-72-2,27070-47-9) help_outline Charge 0 Formula C9H15N5O3 InChIKeyhelp_outline FNKQXYHWGSIFBK-RPDRRWSUSA-N SMILEShelp_outline [H][C@@]1(CNc2nc(N)[nH]c(=O)c2N1)[C@@H](O)[C@H](C)O 2D coordinates Mol file for the small molecule Search links Involved in 13 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline 1-O-(1,2-saturated-alkyl)-sn-glycerol Identifier CHEBI:83957 Charge 0 Formula C4H9O3R SMILEShelp_outline OC[C@H](O)COC[*] 2D coordinates Mol file for the small molecule Search links Involved in 1 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline O2 Identifier CHEBI:15379 (CAS: 7782-44-7) help_outline Charge 0 Formula O2 InChIKeyhelp_outline MYMOFIZGZYHOMD-UHFFFAOYSA-N SMILEShelp_outline O=O 2D coordinates Mol file for the small molecule Search links Involved in 2,648 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline (6R)-L-erythro-6,7-dihydrobiopterin Identifier CHEBI:43120 (CAS: 79647-29-3) help_outline Charge 0 Formula C9H13N5O3 InChIKeyhelp_outline ZHQJVZLJDXWFFX-RPDRRWSUSA-N SMILEShelp_outline C1=2C(=N[C@H](CN1)[C@H]([C@H](C)O)O)C(N=C(N2)N)=O 2D coordinates Mol file for the small molecule Search links Involved in 6 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline a 1-(1-hydroxyalkyl)-sn-glycerol Identifier CHEBI:73418 Charge 0 Formula C4H9O4R SMILEShelp_outline OC[C@H](O)COC(O)[*] 2D coordinates Mol file for the small molecule Search links Involved in 2 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H2O Identifier CHEBI:15377 (Beilstein: 3587155; CAS: 7732-18-5) help_outline Charge 0 Formula H2O InChIKeyhelp_outline XLYOFNOQVPJJNP-UHFFFAOYSA-N SMILEShelp_outline [H]O[H] 2D coordinates Mol file for the small molecule Search links Involved in 6,048 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
RHEA:36255 | RHEA:36256 | RHEA:36257 | RHEA:36258 | |
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Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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Identification of the gene encoding alkylglycerol monooxygenase defines a third class of tetrahydrobiopterin-dependent enzymes.
Watschinger K., Keller M.A., Golderer G., Hermann M., Maglione M., Sarg B., Lindner H.H., Hermetter A., Werner-Felmayer G., Konrat R., Hulo N., Werner E.R.
Alkylglycerol monooxygenase (glyceryl-ether monooxygenase, EC 1.14.16.5) is the only enzyme known to cleave the O-alkyl bond of ether lipids which are essential components of brain membranes, protect the eye from cataract, interfere or mediate signalling processes, and are required for spermatogen ... >> More
Alkylglycerol monooxygenase (glyceryl-ether monooxygenase, EC 1.14.16.5) is the only enzyme known to cleave the O-alkyl bond of ether lipids which are essential components of brain membranes, protect the eye from cataract, interfere or mediate signalling processes, and are required for spermatogenesis. Along with phenylalanine hydroxylase, tyrosine hydroxylase, tryptophan hydroxylase, and nitric oxide synthase, alkylglycerol monooxygenase is one of five known enzymatic reactions which depend on tetrahydrobiopterin. Although first described in 1964, no sequence had been assigned to this enzyme so far since it lost activity upon protein purification attempts. A functional library screen using pools of plasmids of a rat liver expression library transfected to CHO cells was also unsuccessful. We therefore selected human candidate genes by bioinformatic approaches and by proteomic analysis of partially purified enzyme and tested alkylglycerol monooxygenase activity in CHO cells transfected with expression plasmids. Transmembrane protein 195, a predicted membrane protein with unassigned function which occurs in bilateral animals, was found to encode for tetrahydrobiopterin-dependent alkylglycerol monooxygenase. This sequence assignment was confirmed by injection of transmembrane protein 195 cRNA into Xenopus laevis oocytes. Transmembrane protein 195 shows no sequence homology to aromatic amino acid hydroxylases or nitric oxide synthases, but contains the fatty acid hydroxylase motif. This motif is found in enzymes which contain a diiron center and which carry out hydroxylations of lipids at aliphatic carbon atoms like alkylglycerol monooxygenase. This sequence assignment suggests that alkylglycerol monooxygenase forms a distinct third group among tetrahydrobiopterin-dependent enzymes. << Less
Proc. Natl. Acad. Sci. U.S.A. 107:13672-13677(2010) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.
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Tetrahydropteridine-dependent cleavage enzyme for O-alkyl lipids: substrate specificity.
Snyder F., Malone B., Piantadosi C.
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Glyceryl-ether monooxygenase [EC 1.14.16.5]. A microsomal enzyme of ether lipid metabolism.
Taguchi H., Armarego W.L.
The history, biological, and medical aspects of glyceryl ethers, as well as their chemical syntheses, biosynthesis, and their chemical and physical properties are briefly reviewed as background information for appreciating the importance of the enzyme glyceryl-ether monooxygenase, and for embarkin ... >> More
The history, biological, and medical aspects of glyceryl ethers, as well as their chemical syntheses, biosynthesis, and their chemical and physical properties are briefly reviewed as background information for appreciating the importance of the enzyme glyceryl-ether monooxygenase, and for embarking on new studies of this enzyme. The occurrence, isolation and general properties of the microsomal, membrane-bound, glyceryl-ether monooxygenase from rat liver are described. Radiometric, nonradiometric, and coupled and direct spectrophotometric assays for this enzyme are detailed. The effects of detergents on the kinetics of this enzyme are described together with the stoichiometry and the effects of inhibitors. The structure-activity relationships of pterin cofactors and of ether lipid substrates, including their stereospecificities, have been summarized from enzyme kinetic data which are also tabulated. The mechanism of enzymic hydroxylation of glyceryl ethers and a model for the active site of glyceryl-ether monooxygenase are proposed from these apparent kinetic data. Notes on useful future studies of this monooxygenase have been made. << Less