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

Fern R. McSorley; Peter W. Wyatt; Ascuncion Martinez; Edward F. DeLong; Bjarne Hove-Jensen; David L. Zechel

doi:10.1021/ja302072f

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

Fern R. McSorley
, Peter W. Wyatt
, Ascuncion Martinez
, Edward F. DeLong
, Bjarne Hove-Jensen
, David L. Zechel

Queen's University
University of London
Massachusetts Institute of Technology, Cambridge, Massachusetts, USA

Research output: Contribution to journal › Journal article › Research › peer-review

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.

Original language	English
Journal	American Chemical Society. Journal
Volume	134
Issue number	20
Pages (from-to)	8364-8367
Number of pages	4
ISSN	0002-7863
DOIs	https://doi.org/10.1021/ja302072f
Publication status	Published - 23 May 2012

Access to Document

10.1021/ja302072f

Cite this

@article{ecc7a68f3ece4b4d89c37e9f08588b5a,

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

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.",

author = "McSorley, \{Fern R.\} and Wyatt, \{Peter W.\} and Ascuncion Martinez and DeLong, \{Edward F.\} and Bjarne Hove-Jensen and Zechel, \{David L.\}",

year = "2012",

month = may,

day = "23",

doi = "10.1021/ja302072f",

language = "English",

volume = "134",

pages = "8364--8367",

journal = "American Chemical Society. Journal",

issn = "0002-7863",

publisher = "American Chemical Society",

number = "20",

}

TY - JOUR

T1 - PhnY and PhnZ comprise a new oxidative pathway for enzymatic cleavage of a carbon-phosphorus bond

AU - McSorley, Fern R.

AU - Wyatt, Peter W.

AU - Martinez, Ascuncion

AU - DeLong, Edward F.

AU - Hove-Jensen, Bjarne

AU - Zechel, David L.

PY - 2012/5/23

Y1 - 2012/5/23

N2 - 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.

AB - 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.

U2 - 10.1021/ja302072f

DO - 10.1021/ja302072f

M3 - Journal article

SN - 0002-7863

VL - 134

SP - 8364

EP - 8367

JO - American Chemical Society. Journal

JF - American Chemical Society. Journal

IS - 20

ER -

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

Abstract

Access to Document

Fingerprint

Cite this