PhnY and PhnZ Comprise a New Oxidative Pathway for Enzymatic Cleavage of a Carbon–Phosphorus Bond

The sequential activities of PhnY, an α-ketoglutarate/Fe(II)-dependent dioxygenase, and PhnZ, a Fe(II)-dependent enzyme of the histidine-aspartate motif hydrolase family, cleave the carbon–phosphorus bond of the organophosphonate natural product 2-aminoethylphosphonic acid. PhnY adds a hydroxyl grou...

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Bibliographic Details
Published in:Journal of the American Chemical Society 2012-05, Vol.134 (20), p.8364-8367
Main Authors: McSorley, Fern R, Wyatt, Peter B, Martinez, Asuncion, DeLong, Edward F, Hove-Jensen, Bjarne, Zechel, David L
Format: Article
Language:English
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Summary:The sequential activities of PhnY, an α-ketoglutarate/Fe(II)-dependent dioxygenase, and PhnZ, a Fe(II)-dependent enzyme of the histidine-aspartate motif hydrolase family, cleave the carbon–phosphorus bond of the organophosphonate natural product 2-aminoethylphosphonic acid. PhnY adds a hydroxyl group to the α-carbon, yielding 2-amino-1-hydroxyethylphosphonic acid, which is oxidatively converted by PhnZ to inorganic phosphate and glycine. The PhnZ reaction represents a new enzyme mechanism for metabolic cleavage of a carbon–phosphorus bond.
ISSN:0002-7863
1520-5126
DOI:10.1021/ja302072f