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Evidence that oxidative dephosphorylation by the nonheme Fe( II), α-ketoglutarate: UMP oxygenase occurs by stereospecific hydroxylation.
- Source :
-
FEBS Letters . Feb2017, Vol. 591 Issue 3, p468-478. 11p. - Publication Year :
- 2017
-
Abstract
- LipL and Cpr19 are nonheme, mononuclear Fe( II)-dependent, α-ketoglutarate (α KG): UMP oxygenases that catalyze the formation of CO2, succinate, phosphate, and uridine-5′-aldehyde, the last of which is a biosynthetic precursor for several nucleoside antibiotics that inhibit bacterial translocase I (MraY). To better understand the chemistry underlying this unusual oxidative dephosphorylation and establish a mechanistic framework for LipL and Cpr19, we report herein the synthesis of two biochemical probes-[1′,3′,4′,5′,5′-2H] UMP and the phosphonate derivative of UMP-and their activity with both enzymes. The results are consistent with a reaction coordinate that proceeds through the loss of one 2H atom of [1′,3′,4′,5′,5′-2H] UMP and stereospecific hydroxylation geminal to the phosphoester to form a cryptic intermediate, (5′ R)-5′-hydroxy- UMP. Thus, these enzyme catalysts can additionally be assigned as UMP hydroxylase-phospholyases. [ABSTRACT FROM AUTHOR]
- Subjects :
- *DEPHOSPHORYLATION
*GLUTARIC acid
*STEREOSPECIFICITY
*HYDROXYLATION
*OXYGENASES
Subjects
Details
- Language :
- English
- ISSN :
- 00145793
- Volume :
- 591
- Issue :
- 3
- Database :
- Academic Search Index
- Journal :
- FEBS Letters
- Publication Type :
- Academic Journal
- Accession number :
- 121289395
- Full Text :
- https://doi.org/10.1002/1873-3468.12554