Document Detail


Uncovering novel biochemistry in the mechanism of tryptophan tryptophylquinone cofactor biosynthesis.
MedLine Citation:
PMID:  19648051     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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.
Authors:
Carrie M Wilmot; Victor L Davidson
Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Review     Date:  2009-08-03
Journal Detail:
Title:  Current opinion in chemical biology     Volume:  13     ISSN:  1879-0402     ISO Abbreviation:  Curr Opin Chem Biol     Publication Date:  2009 Oct 
Date Detail:
Created Date:  2009-09-23     Completed Date:  2010-01-27     Revised Date:  2014-09-16    
Medline Journal Info:
Nlm Unique ID:  9811312     Medline TA:  Curr Opin Chem Biol     Country:  England    
Other Details:
Languages:  eng     Pagination:  469-74     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Coenzymes / metabolism
Indolequinones / metabolism*
Oxidoreductases Acting on CH-NH Group Donors / metabolism*
Paracoccus denitrificans / enzymology*
Tryptophan / analogs & derivatives*,  metabolism
Grant Support
ID/Acronym/Agency:
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:
0/Coenzymes; 0/Indolequinones; 134645-25-3/tryptophan tryptophylquinone; 8DUH1N11BX/Tryptophan; EC 1.4.9.1/methylamine dehydrogenase; EC 1.5.-/Oxidoreductases Acting on CH-NH Group Donors
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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