4xb6

Structural highlights

Function

[PHNJ_ECOLI] Catalyzes the breakage of the C-P bond in alpha-D-ribose 1-methylphosphonate 5-phosphate (PRPn) forming alpha-D-ribose 1,2-cyclic phosphate 5-phosphate (PRcP).^[1] [PHNG_ECOLI] Together with PhnH, PhnI and PhnL is required for the transfer of the ribose triphosphate moiety from ATP to methyl phosphonate.^[2] [PHNI_ECOLI] Together with PhnG, PhnH and PhnL is required for the transfer of the ribose triphosphate moiety from ATP to methyl phosphonate. PhnI alone has nucleosidase activity, catalyzing the hydrolysis of ATP or GTP forming alpha-D-ribose 5-triphosphate and adenine or guanine, respectively.^[3] [PHNH_ECOLI] Together with PhnG, PhnI and PhnL is required for the transfer of the ribose triphosphate moiety from ATP to methyl phosphonate.^[4]

References

1. ↑ Kamat SS, Williams HJ, Raushel FM. Intermediates in the transformation of phosphonates to phosphate by bacteria. Nature. 2011 Nov 16;480(7378):570-3. doi: 10.1038/nature10622. PMID:22089136 doi:http://dx.doi.org/10.1038/nature10622
2. ↑ Kamat SS, Williams HJ, Raushel FM. Intermediates in the transformation of phosphonates to phosphate by bacteria. Nature. 2011 Nov 16;480(7378):570-3. doi: 10.1038/nature10622. PMID:22089136 doi:http://dx.doi.org/10.1038/nature10622
3. ↑ Kamat SS, Williams HJ, Raushel FM. Intermediates in the transformation of phosphonates to phosphate by bacteria. Nature. 2011 Nov 16;480(7378):570-3. doi: 10.1038/nature10622. PMID:22089136 doi:http://dx.doi.org/10.1038/nature10622
4. ↑ Kamat SS, Williams HJ, Raushel FM. Intermediates in the transformation of phosphonates to phosphate by bacteria. Nature. 2011 Nov 16;480(7378):570-3. doi: 10.1038/nature10622. PMID:22089136 doi:http://dx.doi.org/10.1038/nature10622