| Glyceryl ether monooxygenase resembles aromatic amino acid hydroxylases in metal ion and tetrahydrobiopterin dependence. | |
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MedLine Citation:
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PMID: 19007315 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Glyceryl ether monooxygenase is a tetrahydrobiopterin-dependent membrane-bound enzyme which catalyses the cleavage of lipid ethers into glycerol and the corresponding aldehyde. Despite many different characterisation and purification attempts, so far no gene and primary sequence have been assigned to this enzyme. The seven other tetrahydrobiopterin-dependent enzymes can be divided in the family of aromatic amino acid hydroxylases - comprising phenylalanine hydroxylase, tyrosine hydroxylase and the two tryptophan hydroxylases - and into the three nitric oxide synthases. We tested the influences of different metal ions and metal ion chelators on glyceryl ether monooxygenase, phenylalanine hydroxylase and nitric oxide synthase activity to elucidate the relationship of glyceryl ether monooxygenase to these two families. 1,10-Phenanthroline, an inhibitor of non-heme iron-dependent enzymes, was able to potently block glyceryl ether monooxygenase as well as phenylalanine hydroxylase, but had no effect on inducible nitric oxide synthase. Two tetrahydrobiopterin analogues, N(5)-methyltetrahydrobiopterin and 4-aminotetrahydrobiopterin, had a similar impact on glyceryl ether monooxygenase activity, as has already been shown for phenylalanine hydroxylase. These observations point to a close analogy of the role of tetrahydrobiopterin in glyceryl ether monooxygenase and in aromatic amino acid hydroxylases and suggest that glyceryl ether monooxygenase may require a non-heme iron for catalysis. |
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Authors:
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Katrin Watschinger; Markus A Keller; Albin Hermetter; Georg Golderer; Gabriele Werner-Felmayer; Ernst R Werner |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: Biological chemistry Volume: 390 ISSN: 1431-6730 ISO Abbreviation: Biol. Chem. Publication Date: 2009 Jan |
Date Detail:
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Created Date: 2008-12-17 Completed Date: 2009-03-12 Revised Date: 2013-03-27 |
Medline Journal Info:
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Nlm Unique ID: 9700112 Medline TA: Biol Chem Country: Germany |
Other Details:
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Languages: eng Pagination: 3-10 Citation Subset: IM |
Affiliation:
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Division of Biological Chemistry, Biocentre, Innsbruck Medical University, Fritz-Pregl-Str. 3/VI, A-6020 Innsbruck, Austria. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Amino Acids, Aromatic
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metabolism* Animals Binding, Competitive Biopterin / analogs & derivatives*, metabolism, pharmacology Cell Line Edetic Acid / pharmacology Enzyme Activation / drug effects Glyceryl Ethers / metabolism* Liver / cytology Metals / metabolism*, pharmacology Mice Microsomes / chemistry, drug effects, enzymology Mixed Function Oxygenases / antagonists & inhibitors, metabolism* Nitric Oxide Synthase / metabolism Phenanthrolines / pharmacology Phenylalanine Hydroxylase / antagonists & inhibitors, metabolism Rats Reproducibility of Results Solubility |
| Grant Support | |
ID/Acronym/Agency:
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P 19764-B05//Austrian Science Fund FWF |
| Chemical | |
Reg. No./Substance:
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0/Amino Acids, Aromatic; 0/Glyceryl Ethers; 0/Metals; 0/Phenanthrolines; 17528-72-2/5,6,7,8-tetrahydrobiopterin; 22150-76-1/Biopterin; 60-00-4/Edetic Acid; EC 1.-/Mixed Function Oxygenases; EC 1.14.13.39/Nitric Oxide Synthase; EC 1.14.16.1/Phenylalanine Hydroxylase; W4X6ZO7939/1,10-phenanthroline |
| Comments/Corrections | |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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