PMID:19788654

Martinez A, Tyson GW, Delong EF

Widespread known and novel phosphonate utilization pathways in marine bacteria revealed by functional screening and metagenomic analyses.

Environ Microbiol 12:222-38 (2010)
DOI:10.1111/j.1462-2920.2009.02062.x

[ag:ACU83549]

PMID:22564006

McSorley FR, Wyatt PB, Martinez A, DeLong EF, Hove-Jensen B, Zechel DL

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

J Am Chem Soc 134:8364-7 (2012)
DOI:10.1021/ja302072f

Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
With 2-oxoglutarate as one donor, and incorporation of one atom of oxygen into each donor
BRITE hierarchy

(2-aminoethyl)phosphonate,2-oxoglutarate:oxygen oxidoreductase (1-hydroxylating)

(2-aminoethyl)phosphonate + 2-oxoglutarate + O2 = (2-amino-1-hydroxyethyl)phosphonate + succinate + CO2 [RN:R10724]

R10724
Reaction

(2-aminoethyl)phosphonate [CPD:C03557];
2-oxoglutarate [CPD:C00026];
O2 [CPD:C00007]

Requires Fe2+ and ascorbate. The enzyme, characterized from an uncultured marine bacterium, is involved in a (2-aminoethyl)phosphonate degradation pathway.

EC 1.14.11.46 created 2014

1  [PMID:22564006]

McSorley FR, Wyatt PB, Martinez A, DeLong EF, Hove-Jensen B, Zechel DL

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

J Am Chem Soc 134:8364-7 (2012)
DOI:10.1021/ja302072f