Intermediates in the transformation of phosphonates to phosphate by bacteria

Kamat, Siddhesh S.; Williams, Howard J.; Raushel, Frank M.

doi:10.1038/nature10622

Cited by 126 publications

(155 citation statements)

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“…Spectroscopy revealed the possibility of a 4Fe-4S cluster, and with the observation of the presence of four cysteine residues within PhnJ, the data are consistent with a radical reaction mechanism typical of the radical S-adenosylmethionine/4Fe-4S enzyme superfamily. Three cysteine residues (Cys241, Cys244, and Cys266) are involved in the formation of the 4Fe-4S cluster, whereas Cys272 is believed to take part in the catalytic cycle as a thiyl radical (41,43). Additionally, these data are consistent with results obtained Ͼ2 decades ago by Frost and coworkers, who demonstrated that C-P bond cleavage by C-P lyase occurs by a radical reaction mechanism (44)(45)(46).…”

Section: Mesorhizobium Lotisupporting

confidence: 81%

“…No enzymatic activity of PhnGHIJK was demonstrated, but in vitro analysis has shown that PhnI has ribonucleoside 5=-triphosphate nucleosidase activity (ATP/ GTP ϩ H 2 O ¡ ribosyl 5-triphosphate ϩ adenine/guanine), whereas PhnI in the presence of PhnG, PhnH, and PhnL has ribonucleoside 5=-triphosphate phosphonylase activity (ATP/GTP ϩ methylphosphonic acid ¡ 5=-triphosphoribosyl 1=-methylphosphonate ϩ adenine/guanine) (EC 2.7. ) (41). The phosphonylase activity is dependent on the presence of PhnG, PhnH, PhnI, and PhnL, whereas PhnK is not necessary.…”

Section: Mesorhizobium Lotimentioning

confidence: 99%

“…The reaction mechanism of the phosphonylase may bear some mechanistic resemblance to that of (deoxy)ribonucleoside phosphorylases, which convert (deoxy)ribonucleoside and P i to ribosyl 1-phosphate and the corresponding nucleic acid base. In the following step of the C-P lyase pathway, the ␤,␥-diphosphoryl group of 5=-triphosphoribosyl 1=-methylphosphonate is hydrolyzed, and 5=-phosphoribosyl 1=-methylphosphonate is generated in a reaction catalyzed by PhnM, hence 5=-triphosphoribosyl 1=-phosphonate diphosphohydrolase (EC 3.6.1.63 [␣-D-ribose 1-methylphosphonate 5-triphosphate diphosphatase]) (41). Similar reactions occur in the catabolism of glyphosate or AMPA (Fig.…”

Section: Mesorhizobium Lotimentioning

confidence: 99%

“…Hitherto, the only C-P lyase substrate synthesized is 5=-phosphoribosyl 1=-methylphosphonate (41), and the only C-P lyase substrate isolated from cells is 5=-phosphoribosyl 1=-(2-N-acetamidoethylphosphonate) (39). Such in vitro analyses, which are now available, together with the discovery of the multisubunit Phn-GHIJK protein complex may answer a longstanding question concerning C-P lyase: why are so many gene products required to cleave a C-P bond?…”

Section: Individual Polypeptides and Their Contribution To The C-p Lymentioning

confidence: 99%

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Utilization of Glyphosate as Phosphate Source: Biochemistry and Genetics of Bacterial Carbon-Phosphorus Lyase

Hove‐Jensen

Zechel

Jochimsen

2014

Microbiol Mol Biol Rev

185

157

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SUMMARY After several decades of use of glyphosate, the active ingredient in weed killers such as Roundup, in fields, forests, and gardens, the biochemical pathway of transformation of glyphosate phosphorus to a useful phosphorus source for microorganisms has been disclosed. Glyphosate is a member of a large group of chemicals, phosphonic acids or phosphonates, which are characterized by a carbon-phosphorus bond. This is in contrast to the general phosphorus compounds utilized and metabolized by microorganisms. Here phosphorus is found as phosphoric acid or phosphate ion, phosphoric acid esters, or phosphoric acid anhydrides. The latter compounds contain phosphorus that is bound only to oxygen. Hydrolytic, oxidative, and radical-based mechanisms for carbon-phosphorus bond cleavage have been described. This review deals with the radical-based mechanism employed by the carbon-phosphorus lyase of the carbon-phosphorus lyase pathway, which involves reactions for activation of phosphonate, carbon-phosphorus bond cleavage, and further chemical transformation before a useful phosphate ion is generated in a series of seven or eight enzyme-catalyzed reactions. The phn genes, encoding the enzymes for this pathway, are widespread among bacterial species. The processes are described with emphasis on glyphosate as a substrate. Additionally, the catabolism of glyphosate is intimately connected with that of aminomethylphosphonate, which is also treated in this review. Results of physiological and genetic analyses are combined with those of bioinformatics analyses.

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Section: Mesorhizobium Lotisupporting

confidence: 81%

Section: Mesorhizobium Lotimentioning

confidence: 99%

Section: Mesorhizobium Lotimentioning

confidence: 99%

Section: Individual Polypeptides and Their Contribution To The C-p Lymentioning

confidence: 99%

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Utilization of Glyphosate as Phosphate Source: Biochemistry and Genetics of Bacterial Carbon-Phosphorus Lyase

Hove‐Jensen

Zechel

Jochimsen

2014

Microbiol Mol Biol Rev

185

157

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“…Several lines of evidence support this 'aerobic methane production' hypothesis: (i) the C-P lyase enzyme complex catabolizes MPn to CH 4 , releasing phosphate (P i ) that can be used for growth 10,11 (reviewed in White and Metcalf 12 ); (ii) C-P lyase gene sequences are present (sometimes abundant) in marine environments [13][14][15][16][17] ; (iii) natural seawater samples incubated with MPn release CH 4 9,17 ; (iv) biosynthesis of MPn by Nitrosopumilus maritimus SCM1, a member of the ubiquitous and abundant Marine Group I (MGI) archaea was recently demonstrated 18 ; and (v) ca. 0.6% of microbes in marine surface communities contain genes encoding the MPn synthase 18 .…”

mentioning

confidence: 99%

Methane production by phosphate-starved SAR11 chemoheterotrophic marine bacteria

et al. 2014

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The oxygenated surface waters of the world's oceans are supersaturated with methane relative to the atmosphere, a phenomenon termed the 'marine methane paradox'. The production of methylphosphonic acid (MPn) by marine archaea related to Nitrosopumilus maritimus and subsequent decomposition of MPn by phosphate-starved bacterioplankton may partially explain the excess methane in surface waters. Here we show that Pelagibacterales sp. strain HTCC7211, an isolate of the SAR11 clade of marine a-proteobacteria, produces methane from MPn, stoichiometric to phosphorus consumption, when starved for phosphate. Gene transcripts encoding phosphonate transport and hydrolysis proteins are upregulated under phosphate limitation, suggesting a genetic basis for the methanogenic phenotype. Strain HTCC7211 can also use 2-aminoethylphosphonate and assorted phosphate esters for phosphorus nutrition. Despite strain-specific differences in phosphorus utilization, these findings identify Pelagibacterales bacteria as a source of biogenic methane and further implicate phosphate starvation of chemoheterotrophic bacteria in the long-observed methane supersaturation in oxygenated waters.

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Congener‐Induced Sulfur‐Related Metabolism Interference Therapy Promoted by Photothermal Sensitization for Combating Bacteria

Ding

Luo

et al. 2021

Advanced Materials

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of biosynthesis, energy conversion, life activities, and stress resistance. [1] As prokaryotes facing environment independently, pathogen bacteria exhibit stronger metabolic homeostasis and thus achieve stronger stress resistance than human cells, allowing them causing persistent harm to human hosts. [2,3] In implantassociated infection (IAI) conditions, the intervention of biofilm, known as bacteria communities, enables bacteria to achieve better metabolic homeostasis and stronger antimicrobial resistance, becoming a common clinical dilemma. [4,5] Therefore, effectively destroying bacterial metabolic homeostasis is of great significance to bacteria killing, especially in IAI. The current antibiotics are mainly aiming at breaking the function of a specific target, such as cell membranes, cell walls, ribosomes, and transcription processes, which is more likely to cause bacterial resistance endangering public health. [6] However, few studies have been enabled to focus on the disruption of bacteria metabolic homeostasis in biochemical metabolic processes.Biochemical properties of essential elements, such as nitrogen (N), phosphorus (P), S, Se, and calcium (Ca), play important roles in intracellular biochemical reactions, and thus tightly connect with the regulation of cell metabolic state. [7] Interestingly, some congeners in the periodic table, S and Se, as well as Ca and strontium (Sr), have similar biochemical properties and share similar metabolic functions. [8] Among them, S and Se, two vital trace elements, exhibit intense and extensive reaction competition in cell metabolism, owning to their extremely similar biochemical properties as congeners. [9] Moreover, we found a definite biological diversity that bacterial cells can utilize inorganic S and Se, while human cells cannot. [10,11] H 2 S is the key metabolic intermediate in the pathway of inorganic S transformation and utilization in bacteria. [9] Meanwhile, H 2 Se shares all the same catalyzing enzymes and forms the homologous substituents with H 2 S in this pathway. [9,11,12] This mechanism makes it possible to allow intracellular overloaded H 2 Se for intervening with entire downstream sulfur-related metabolism state with cascade amplification and further destruction of bacteria metabolism Metabolic homeostasis is vital for individual cells to keep alive. Stronger metabolic homeostasis allows bacteria to survive in vivo and do persistent harm to hosts, which is especially typical in implant-associated infection (IAI) with biofilm intervention. Herein, based on the competitive role of selenium (Se) and sulfur (S) in bacteria metabolism as congeners, a congener-induced sulfur-related metabolism interference therapy (SMIT) eradicating IAI is proposed by specific destruction of bacteria metabolic homeostasis. The original nanodrug manganese diselenide (MnSe 2 ) is devised to generate permeable H 2 Se in bacteria, triggered by the acidic microenvironment. H 2 Se, the congener substitution of H 2 S, as a bacteria-specific intermediate metabolite, can embe...

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Intermediates in the transformation of phosphonates to phosphate by bacteria

Cited by 126 publications

References 26 publications

Utilization of Glyphosate as Phosphate Source: Biochemistry and Genetics of Bacterial Carbon-Phosphorus Lyase

Utilization of Glyphosate as Phosphate Source: Biochemistry and Genetics of Bacterial Carbon-Phosphorus Lyase

Methane production by phosphate-starved SAR11 chemoheterotrophic marine bacteria

Congener‐Induced Sulfur‐Related Metabolism Interference Therapy Promoted by Photothermal Sensitization for Combating Bacteria

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