| Uncovering novel biochemistry in the mechanism of tryptophan tryptophylquinone cofactor biosynthesis. | |
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MedLine Citation:
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PMID: 19648051 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Catalytic quinone cofactors derived from post-translational modification of amino acid residues within the enzyme polypeptide have roles in a variety of biological processes ranging from metabolism in bacteria to inflammation and connective tissue maturation in humans. In recent years, studies of the biosynthesis of one of these cofactors, tryptophan tryptophylquinone (TTQ), have provided examples of novel chemistry that is required for the generation of these protein-derived cofactors. A novel c-type diheme enzyme, MauG, catalyzes a six-electron oxidation that completes TTQ biosynthesis in a 119-kDa protein substrate. The post-translational modification reactions proceed via an unprecedented Fe(V) equivalent catalytic intermediate comprising two hemes; one an Fe(IV)=O and the other a six-coordinate Fe(IV) with axial ligands provided by amino acid residues. This high-valent diheme species is an alternative to Compound I, an Fe(IV)=O heme with a porphyrin or amino acid cation radical, which is typically the reactive intermediate of heme-dependent oxygenases and peroxidases. |
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Authors:
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Carrie M Wilmot; Victor L Davidson |
Publication Detail:
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Type: Journal Article; Research Support, N.I.H., Extramural; Review Date: 2009-08-03 |
Journal Detail:
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Title: Current opinion in chemical biology Volume: 13 ISSN: 1879-0402 ISO Abbreviation: Curr Opin Chem Biol Publication Date: 2009 Oct |
Date Detail:
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Created Date: 2009-09-23 Completed Date: 2010-01-27 Revised Date: 2013-05-08 |
Medline Journal Info:
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Nlm Unique ID: 9811312 Medline TA: Curr Opin Chem Biol Country: England |
Other Details:
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Languages: eng Pagination: 469-74 Citation Subset: IM |
Affiliation:
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Department of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, 321 Church Street SE, Minneapolis, MN 55455, USA. wilmo004@umn.edu |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Coenzymes
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metabolism Indolequinones / metabolism* Oxidoreductases Acting on CH-NH Group Donors / metabolism* Paracoccus denitrificans / enzymology* Tryptophan / analogs & derivatives*, metabolism |
| Grant Support | |
ID/Acronym/Agency:
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GM-41574/GM/NIGMS NIH HHS; GM-66569/GM/NIGMS NIH HHS; R01 GM041574/GM/NIGMS NIH HHS; R01 GM041574-21/GM/NIGMS NIH HHS; R01 GM066569/GM/NIGMS NIH HHS; R01 GM066569-07/GM/NIGMS NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Coenzymes; 0/Indolequinones; 134645-25-3/tryptophan tryptophylquinone; 73-22-3/Tryptophan; EC 1.4.9.1/methylamine dehydrogenase; EC 1.5.-/Oxidoreductases Acting on CH-NH Group Donors |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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