| Structural highlights
Function
PHNZ_UNCHF Involved in the degradation of the organophosphonate 2-aminoethylphosphonic acid (2-AEP) (Probable). Catalyzes the cleavage of the carbon-phosphorus bond of (2-amino-1-hydroxyethyl)phosphonic acid to yield glycine and phosphate through an oxidative mechanism (PubMed:22564006, PubMed:24198335, PubMed:24706911). It reacts stereospecifically with the R-enantiomer of (2-amino-1-hydroxyethyl)phosphonic acid and is also able to use (R,R)-2-amino-1-hydroxypropylphosphonate as substrate (PubMed:24706911).[1] [2] [3] [4]
Publication Abstract from PubMed
The founding members of the HD-domain protein superfamily are phosphohydrolases, and newly discovered members are generally annotated as such. However, myo-inositol oxygenase (MIOX) exemplifies a second, very different function that has evolved within the common scaffold of this superfamily. A recently discovered HD protein, PhnZ, catalyzes conversion of 2-amino-1-hydroxyethylphosphonate to glycine and phosphate, culminating a bacterial pathway for the utilization of environmentally abundant 2-aminoethylphosphonate. Using Mossbauer and EPR spectroscopies, X-ray crystallography, and activity measurements, we show here that, like MIOX, PhnZ employs a mixed-valent Fe(II)/Fe(III) cofactor for the O2-dependent oxidative cleavage of its substrate. Phylogenetic analysis suggests that many more HD proteins may catalyze yet-unknown oxygenation reactions using this hitherto exceptional Fe(II)/Fe(III) cofactor. The results demonstrate that the catalytic repertoire of the HD superfamily extends well beyond phosphohydrolysis and suggest that the mechanism used by MIOX and PhnZ may be a common strategy for oxidative C-X bond cleavage.
Organophosphonate-degrading PhnZ reveals an emerging family of HD domain mixed-valent diiron oxygenases.,Worsdorfer B, Lingaraju M, Yennawar NH, Boal AK, Krebs C, Bollinger JM Jr, Pandelia ME Proc Natl Acad Sci U S A. 2013 Nov 19;110(47):18874-9. doi:, 10.1073/pnas.1315927110. Epub 2013 Nov 6. PMID:24198335[5]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ 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. 2012 May 23;134(20):8364-7. doi: 10.1021/ja302072f. Epub 2012 May , 11. PMID:22564006 doi:http://dx.doi.org/10.1021/ja302072f
- ↑ Worsdorfer B, Lingaraju M, Yennawar NH, Boal AK, Krebs C, Bollinger JM Jr, Pandelia ME. Organophosphonate-degrading PhnZ reveals an emerging family of HD domain mixed-valent diiron oxygenases. Proc Natl Acad Sci U S A. 2013 Nov 19;110(47):18874-9. doi:, 10.1073/pnas.1315927110. Epub 2013 Nov 6. PMID:24198335 doi:http://dx.doi.org/10.1073/pnas.1315927110
- ↑ van Staalduinen LM, McSorley FR, Schiessl K, Seguin J, Wyatt PB, Hammerschmidt F, Zechel DL, Jia Z. Crystal structure of PhnZ in complex with substrate reveals a di-iron oxygenase mechanism for catabolism of organophosphonates. Proc Natl Acad Sci U S A. 2014 Apr 8;111(14):5171-6. doi:, 10.1073/pnas.1320039111. Epub 2014 Mar 21. PMID:24706911 doi:http://dx.doi.org/10.1073/pnas.1320039111
- ↑ 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. 2010 Jan;12(1):222-38. doi: 10.1111/j.1462-2920.2009.02062.x. , Epub 2009 Sep 29. PMID:19788654 doi:http://dx.doi.org/10.1111/j.1462-2920.2009.02062.x
- ↑ Worsdorfer B, Lingaraju M, Yennawar NH, Boal AK, Krebs C, Bollinger JM Jr, Pandelia ME. Organophosphonate-degrading PhnZ reveals an emerging family of HD domain mixed-valent diiron oxygenases. Proc Natl Acad Sci U S A. 2013 Nov 19;110(47):18874-9. doi:, 10.1073/pnas.1315927110. Epub 2013 Nov 6. PMID:24198335 doi:http://dx.doi.org/10.1073/pnas.1315927110
|
