PhnY and PhnZ comprise a new oxidative pathway for enzymatic cleavage of a carbon-phosphorus bond

Journal of the American Chemical Society
Fern R McSorleyDavid L Zechel

Abstract

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.

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Citations

May 16, 2013·Journal of the American Chemical Society·Wei-chen ChangHung-wen Liu
Apr 8, 2014·Proceedings of the National Academy of Sciences of the United States of America·Laura M van StaalduinenZongchao Jia
Feb 3, 2016·Current Opinion in Chemical Biology·Jason P ChinJohn P Quinn
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Jan 11, 2014·Annual Review of Marine Science·David M Karl
Nov 8, 2013·Proceedings of the National Academy of Sciences of the United States of America·Bigna WörsdörferMaria-Eirini Pandelia
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Feb 28, 2019·ACS Chemical Biology·Simanga R GamaDavid L Zechel

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