Determination of 2-aminoethylphosphonic acid and its N-methyl derivative in animal tissues by gas chromatography with flame photometric detection.

Kataoka, Hiroyuki; Sakiyama, Norihisa; Makita, Masami

doi:10.1271/bbb1961.53.2791

Cited by 7 publications

(4 citation statements)

References 10 publications

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“…While 2-AEP is the most abundant phosphonate in nature, TMAEP, as well as DMAEP and N -methyl-AEP, have been reported in protozoa and marine invertebrates such as sea anemones, marine plankton, and algae. 114,116–118 Degradation pathways for both 2-AEP and phosphonoalanine have been discovered, ultimately producing phosphate and a source of carbon. 119–123 The TmpA/B pathway mirrors the PhnY/Z degradation pathway for 2-AEP in its chemical transformations but is instead specific for TMAEP.…”

Section: Discussionmentioning

confidence: 99%

A New Microbial Pathway for Organophosphonate Degradation Catalyzed by Two Previously Misannotated Non-Heme-Iron Oxygenases

et al. 2019

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The assignment of biochemical functions to hypothetical proteins is challenged by functional diversification within many protein structural superfamilies. This diversification, which is particularly common for metalloenzymes, renders functional annotations that are founded solely on sequence and domain similarities unreliable and often erroneous. Definitive biochemical characterization to delineate functional sub-groups within these superfamilies will aid in improving bioinformatic approaches for functional annotation. We describe here the structural and functional characterization of two non-heme-iron oxygenases, TmpA and TmpB, which are encoded by a genomically clustered pair of genes found in more than 350 species of bacteria. TmpA and TmpB are functional homologues of a pair of enzymes (PhnY and PhnZ) that degrade 2-aminoethylphosphonate but instead act on its naturally occurring, quaternary ammonium analogue, 2-(trimethylammonio)ethylphosphonate (TMAEP). TmpA, an iron(II)- and 2-(oxo)glutarate-dependent oxygenase misannotated as a γ-butyrobetaine (γbb) hydroxylase, shows no activity toward γbb but efficiently hydroxylates TMAEP. The product, (R)-1-hydroxy-2-(trimethylammonio)ethylphosphonate [(R)-OH-TMAEP], then serves as the substrate for the second enzyme, TmpB. By contrast to its purported phosphohydrolytic activity, TmpB is an HD-domain oxygenase that uses a mixed-valent diiron cofactor to enact oxidative cleavage of the C–P bond of its substrate, yielding glycine betaine and phosphate. The high specificities of TmpA and TmpB for their N-trimethylated substrates suggests that they have evolved specifically to degrade TMAEP, which was not previously known to be subject to microbial catabolism. This study thus adds to the growing list of known pathways through which microbes break down organophosphonates to harvest phosphorus, carbon, and nitrogen in nutrient-limited niches.

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Section: Discussionmentioning

confidence: 99%

A New Microbial Pathway for Organophosphonate Degradation Catalyzed by Two Previously Misannotated Non-Heme-Iron Oxygenases

et al. 2019

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“…In particular, they could act on the N -methyl derivative of AEP (M 1 AEP), which is reportedly quite common in nature. 27 , 28 , 29 , 30 , 31 , 32 , 33 This compound cannot be processed by PhnW, which—like all PLP-dependent transaminases—requires a substrate with a primary amino group. We thus envisaged that the FAD-dependent oxidoreductases might carry out the reaction shown in Scheme 1 .…”

Section: Resultsmentioning

confidence: 99%

“…This activity seems biologically well justified: M 1 AEP is frequently found in nature (where its abundance can sometimes approach that of AEP 28 , 31 ) but it cannot serve as a substrate for PhnW and therefore it cannot directly enter the pathways shown in Figure 1 . Thus, collectively, the PbfB, PbfC, and PbfD enzymes serve to funnel M 1 AEP into the hydrolytic AEP degradation pathways, allowing the bacteria to consume different aminophosphonates and presumably improving organismal fitness under different nutrient conditions.…”

Section: Discussionmentioning

confidence: 99%

“…However, irrespective of their subgroup, all these proteins showed a substantial similarity to amine oxidoreductases, i.e., enzymes that oxidize various primary and secondary amines, leading to the formation of aldehydes or ketones. 24 , 25 , 26 By analogy, we hypothesized that the identified FAD-dependent enzymes could oxidize some N-alkylated form of AEP, or perhaps of ( R )-HAEP; in particular, they could act on N -methyl AEP (M 1 AEP), which is another frequently found natural product 27 , 28 , 29 , 30 , 31 , 32 , 33 but which cannot be processed by PhnW.…”

Section: Introductionmentioning

confidence: 99%

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Deciphering the role of recurrent FAD-dependent enzymes in bacterial phosphonate catabolism

Zangelmi,

Ruffolo,

Dinhof

et al. 2023

iScience

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Selective and sensitive determination of pamidronate in human plasma and urine by gas chromatography with flame photometric detection

Sakiyama

Kataoka

Makita

1995

Biomedical Chromatography

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A rapid, selective and sensitive method for the determination of pamidronate in human plasma and urine samples by gas chromatography (GC) has been developed. After deproteinization of the sample with trichloroacetic acid, pamidronate was converted into its N-isobutoxycarbonyl methyl ester derivative and measured by GC with flame photometric detection (FPD), using a HP-1 capillary column. The derivative preparation and GC analysis were accomplished within 30 min. The derivative was sufficiently volatile and stable, giving a single and symmetrical peak, and provided an excellent FPD response. The detection limit of pamidronate, at a signal-to-noise ratio of 3, was ca. 100 pg injected, and the calibration curve for this compound in the range 20-1000 ng was linear and sufficiently reproducible for quantitative determination. This method could be successfully applied to plasma and urine samples without a preliminary clean-up except for deproteinization with trichloroacetic acid, and pamidronate could be measured without any influence from coexisting substances. Overall recoveries of pamidronate added to plasma and urine samples were 93-97%. The coefficients of variation for intra-assay and inter-assay of pamidronate in these samples were 1.0-7.9% (n = 3) and 4.1-8.3% (n = 6), respectively.

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Determination of 2-aminoethylphosphonic acid and its N-methyl derivative in animal tissues by gas chromatography with flame photometric detection.

Cited by 7 publications

References 10 publications

A New Microbial Pathway for Organophosphonate Degradation Catalyzed by Two Previously Misannotated Non-Heme-Iron Oxygenases

A New Microbial Pathway for Organophosphonate Degradation Catalyzed by Two Previously Misannotated Non-Heme-Iron Oxygenases

Deciphering the role of recurrent FAD-dependent enzymes in bacterial phosphonate catabolism

Selective and sensitive determination of pamidronate in human plasma and urine by gas chromatography with flame photometric detection

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