• Corpus ID: 19284998

Phosphonates to Phosphate : A Functional Annotation of the Essential Genes of the Phn Operon in Escherichia coli

  title={Phosphonates to Phosphate : A Functional Annotation of the Essential Genes of the Phn Operon in Escherichia coli},
  author={Siddhesh S. Kamat and Howard J. Williams and Frank M. Raushel},
The reaction mechanism for the enzymatic conversion of methyl phosphonate to phosphate and methane in Escherichia coli has eluded researchers over the last three decades despite significant genetic and in vivo studies. The phn operon governs the C-P lyase activity in E. coli. The essential genes within the phn operon are phnGHIJKLM. The proteins encoded by phnGHM were over-expressed in E. coli and purified to homogeneity using standard protocols. The proteins encoded by phnIJKL were soluble… 
Isolation, Biochemical and Genomic Characterization of Glyphosate Tolerant Bacteria to Perform Microbe-Assisted Phytoremediation
An effective strategy is presented of linking the experimental data from the isolation of tolerant bacteria with performing plant-bacteria interaction tests to demonstrate positive effects on the removal of glyphosate from soils.


Escherichia coli phnN, Encoding Ribose 1,5-Bisphosphokinase Activity (Phosphoribosyl Diphosphate Forming): Dual Role in Phosphonate Degradation and NAD Biosynthesis Pathways
An enzymatic pathway for synthesis of 5-phospho-D-ribosyl alpha-1-diphosphate (PRPP) without the participation of PRPP synthase was analyzed in Escherichia coli and the identity of the reaction product as PRPP was confirmed by coupling the ribose 1,5-bisphosphokinase activity to the activity of xanthine phosphoribosyltransferase.
Five phosphonate operon gene products as components of a multi-subunit complex of the carbon-phosphorus lyase pathway
It is concluded that phnGHIJK specify a soluble multisubunit protein complex essential for organophosphonate utilization by Escherichia coli.
Physiological role of phnP-specified phosphoribosyl cyclic phosphodiesterase in catabolism of organophosphonic acids by the carbon-phosphorus lyase pathway.
Results show that 5-phospho-α-D-ribosyl 1,2-cyclic phosphate is an intermediate of organophosphonic acid catabolism, and it is proposed that this compound derives from C-P bond cleavage of 5- PhnP 1-alkylphosphonates by CP lyase.
Rhizobium (Sinorhizobium)meliloti phn Genes: Characterization and Identification of Their Protein Products
The phenotype of this phn mutant shows that the C-P lyase has a broad substrate specificity and that the organism has another enzyme that degrades aminoethylphosphonate, the first in vivo demonstration of the existence of these hitherto hypothetical Phn proteins.
Functional annotation and kinetic characterization of PhnO from Salmonella enterica.
The phnO gene was previously annotated as a transcriptional regulator of unknown function due to sequence homology with members of the GCN5-related N-acyltransferase family (GNAT), but can now be functionally annotation as an aminoalkylphosphonic acid N-acetyltransferase which is able to acetylate a range of aminoalkyphosphonate.
Intermediates in the Transformation of Phosphonates to Phosphate by Bacteria
The elucidation of the chemical steps for the biodegradation of alkylphosphonates shows how these compounds can be metabolized and recycled to phosphate.
Mutational analysis of an Escherichia coli fourteen-gene operon for phosphonate degradation, using TnphoA' elements
The results indicate that the PhnC-to-phnP gene cluster is an operon of 14 genes, and the phnC promoter is the sole psi promoter; three gene products probably constitute a binding protein-dependent Pn transporter; seven gene products are required for catalysis and are likely to constitute a membrane-associated carbon-phosphorus (C-P) lyase; and two gene products may be accessory proteins for the C-P lyase.
Crystal Structure of PhnH: an Essential Component of Carbon-Phosphorus Lyase in Escherichia coli
It is shown that PhnH is essential for C-P bond cleavage in the CP lyase pathway and may be capable of binding negatively charged cyclic compounds through interaction with strictly conserved residues.
Diphthamide biosynthesis requires an organic radical generated by an iron–sulphur enzyme
Archaeal and eukaryotic translation elongation factor 2 contain a unique post-translationally modified histidine residue called diphthamide, which is the target of diphtheria toxin. The biosynthesis