PMID- 22089136
OWN - NLM
STAT- MEDLINE
DCOM- 20120224
LR  - 20211021
IS  - 1476-4687 (Electronic)
IS  - 0028-0836 (Print)
IS  - 0028-0836 (Linking)
VI  - 480
IP  - 7378
DP  - 2011 Nov 16
TI  - Intermediates in the transformation of phosphonates to phosphate by bacteria.
PG  - 570-3
LID - 10.1038/nature10622 [doi]
AB  - Phosphorus is an essential element for all known forms of life. In living 
      systems, phosphorus is an integral component of nucleic acids, carbohydrates and 
      phospholipids, where it is incorporated as a derivative of phosphate. However, 
      most Gram-negative bacteria have the capability to use phosphonates as a 
      nutritional source of phosphorus under conditions of phosphate starvation. In 
      these organisms, methylphosphonate is converted to phosphate and methane. In a 
      formal sense, this transformation is a hydrolytic cleavage of a carbon-phosphorus 
      (C-P) bond, but a general enzymatic mechanism for the activation and conversion 
      of alkylphosphonates to phosphate and an alkane has not been elucidated despite 
      much effort for more than two decades. The actual mechanism for C-P bond cleavage 
      is likely to be a radical-based transformation. In Escherichia coli, the 
      catalytic machinery for the C-P lyase reaction has been localized to the phn gene 
      cluster. This operon consists of the 14 genes phnC, phnD, ..., phnP. Genetic and 
      biochemical experiments have demonstrated that the genes phnG, phnH, ..., phnM 
      encode proteins that are essential for the conversion of phosphonates to 
      phosphate and that the proteins encoded by the other genes in the operon have 
      auxiliary functions. There are no functional annotations for any of the seven 
      proteins considered essential for C-P bond cleavage. Here we show that 
      methylphosphonate reacts with MgATP to form 
      alpha-D-ribose-1-methylphosphonate-5-triphosphate (RPnTP) and adenine. The 
      triphosphate moiety of RPnTP is hydrolysed to pyrophosphate and 
      alpha-D-ribose-1-methylphosphonate-5-phosphate (PRPn). The C-P bond of PRPn is 
      subsequently cleaved in a radical-based reaction producing 
      alpha-D-ribose-1,2-cyclic-phosphate-5-phosphate and methane in the presence of 
      S-adenosyl-L-methionine. Substantial quantities of phosphonates are produced 
      worldwide for industrial processes, detergents, herbicides and pharmaceuticals. 
      Our elucidation of the chemical steps for the biodegradation of alkylphosphonates 
      shows how these compounds can be metabolized and recycled to phosphate.
FAU - Kamat, Siddhesh S
AU  - Kamat SS
AD  - Department of Chemistry, PO Box 30012, Texas A&M University, College Station, 
      Texas 77843, USA.
FAU - Williams, Howard J
AU  - Williams HJ
FAU - Raushel, Frank M
AU  - Raushel FM
LA  - eng
GR  - P01 GM071790/GM/NIGMS NIH HHS/United States
GR  - U54 GM093342-01/GM/NIGMS NIH HHS/United States
GR  - P01 GM071790-07/GM/NIGMS NIH HHS/United States
GR  - GM93342/GM/NIGMS NIH HHS/United States
GR  - GM71790/GM/NIGMS NIH HHS/United States
GR  - U54 GM093342/GM/NIGMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, N.I.H., Extramural
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, Non-P.H.S.
DEP - 20111116
PL  - England
TA  - Nature
JT  - Nature
JID - 0410462
RN  - 0 (Escherichia coli Proteins)
RN  - 0 (Organophosphonates)
RN  - 0 (Phosphates)
RN  - EC 4.- (Lyases)
SB  - IM
MH  - Escherichia coli/enzymology/genetics/*metabolism
MH  - Escherichia coli Proteins/chemistry/genetics
MH  - Lyases/genetics/metabolism
MH  - Organophosphonates/*chemistry/*metabolism
MH  - Phosphates/*chemistry/*metabolism
PMC - PMC3245791
MID - NIHMS330670
COIS- Author Information The authors declare no competing financial interests.
EDAT- 2011/11/18 06:00
MHDA- 2012/03/01 06:00
PMCR- 2012/06/22
CRDT- 2011/11/18 06:00
PHST- 2011/05/02 00:00 [received]
PHST- 2011/10/10 00:00 [accepted]
PHST- 2011/11/18 06:00 [entrez]
PHST- 2011/11/18 06:00 [pubmed]
PHST- 2012/03/01 06:00 [medline]
PHST- 2012/06/22 00:00 [pmc-release]
AID - nature10622 [pii]
AID - 10.1038/nature10622 [doi]
PST - epublish
SO  - Nature. 2011 Nov 16;480(7378):570-3. doi: 10.1038/nature10622.