Document Detail

We two alone will sing: the two-substrate alpha-keto acid-dependent oxygenases.
MedLine Citation:
PMID:  19625206     Owner:  NLM     Status:  MEDLINE    
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.
Panqing He; Graham R Moran
Related Documents :
1979336 - Lack of 3 beta-hydroxy-delta 5-c27-steroid dehydrogenase/isomerase in fibroblasts from ...
1487966 - Isolation and characterization of novel 2-hydroxy fatty acids from the phospholipids of...
19508196 - Synthesis of 4-amino-thiazole analogs of fmoc-amino acids and thiazole linked n-orthogo...
1707236 - Rosenthal fibers share epitopes with alpha b-crystallin, glial fibrillary acidic protei...
7117236 - Effect of ca2+ binding to 5,5'-dithiobis(2-nitrobenzoic acid) light chains on conformat...
6438096 - Synthesis of two hydroxy fatty acids from 7,10,13,16,19-docosapentaenoic acid by human ...
Publication Detail:
Type:  Journal Article; Review     Date:  2009-07-20
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:  -    
Medline Journal Info:
Nlm Unique ID:  9811312     Medline TA:  Curr Opin Chem Biol     Country:  England    
Other Details:
Languages:  eng     Pagination:  443-50     Citation Subset:  IM    
Department of Chemistry and Biochemistry, University of Wisconsin-Milwaukee, 3210 N. Cramer Street, Milwaukee, WI 53211-3029, USA.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
4-Hydroxyphenylpyruvate Dioxygenase / analysis,  antagonists & inhibitors,  metabolism
Crystallography, X-Ray
Dioxygenases / analysis*,  antagonists & inhibitors,  metabolism*
Models, Molecular
Substrate Specificity
Reg. No./Substance:
EC 1.13.11.-/Dioxygenases; EC Dioxygenase

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

Previous Document:  A low-cost thermoelectrically cooled tissue clamp for in vitro cyclic loading and load-to-failure te...
Next Document:  Glycan arrays: recent advances and future challenges.