| We two alone will sing: the two-substrate alpha-keto acid-dependent oxygenases. | |
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MedLine Citation:
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PMID: 19625206 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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4-Hydroxyphenylpyruvate dioxygenase (HPPD) and hydroxymandelate synthase (HMS) are the only two known members of the alpha-keto acid-dependent oxygenases that adopt the fold common to the vicinal oxygen chelate superfamily of enzymes. All other oxygenases of this type have a jellyroll fold. Despite a clearly different ancestry, the salient details of HPPD and HMS catalysis are the same as all alpha-keto acid-dependent oxygenases. All alpha-keto acid-dependent oxygenases use reducing equivalents from an alpha-keto acid to reduce dioxygen via an active site ferrous ion mediator and then catalyze decarboxylation of the alpha-keto acid to promote the formation of a high valence iron-oxo species. The most common purpose of which is to then hydroxylate the substrate. This mini-review summarizes the structural and mechanistic data assembled in recent years for HPPD and HMS in the context of both their roles in nature and the vicinal oxygen chelate and alpha-keto acid-dependent oxygenases superfamilies. |
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Authors:
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Panqing He; Graham R Moran |
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Publication Detail:
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Type: Journal Article; Review Date: 2009-07-20 |
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: - |
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: 443-50 Citation Subset: IM |
Affiliation:
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Department of Chemistry and Biochemistry, University of Wisconsin-Milwaukee, 3210 N. Cramer Street, Milwaukee, WI 53211-3029, USA. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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4-Hydroxyphenylpyruvate Dioxygenase
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analysis,
antagonists & inhibitors,
metabolism Animals Crystallography, X-Ray Dioxygenases / analysis*, antagonists & inhibitors, metabolism* Humans Models, Molecular Substrate Specificity |
| Chemical | |
Reg. No./Substance:
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EC 1.13.11.-/Dioxygenases; EC 1.13.11.27/4-Hydroxyphenylpyruvate Dioxygenase |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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