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

Publikation: Bidrag til tidsskrift › Tidsskriftsartikel › Forskning › 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.

Originalsprog	Engelsk
Tidsskrift	American Chemical Society. Journal
Vol/bind	134
Udgave nummer	20
Sider (fra-til)	8364-8367
Antal sider	4
ISSN	0002-7863
DOI	https://doi.org/10.1021/ja302072f
Status	Udgivet - 23 maj 2012

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10.1021/ja302072f

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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",

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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

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