6881-54-5

Usage

InChI:InChI=1/C2H5O4P/c1-2(3)7(4,5)6/h1H3,(H2,4,5,6)

Upstream product

• 108-24-7 acetic anhydride 
• 75-36-5 acetyl chloride 
• 919-19-7 diethyl acetylphosphonate 
• 17674-28-1 dimethyl acetylphosphonate 
• 6323-97-3 1-aminoethanephosphonic acid 
• 60687-36-7 (R)-(1-aminoethyl)phosphonic acid 
• 1448048-56-3 C₂H₉NO₇P₂ 
• 20188-02-7 (1-hydroxyethyl)phosphonic acid 
• 34550-02-2 1,2-Dihydroxyethylidene-1,1-bis(phosphonic acid) 
• 67532-84-7 dibenzyl acetylphosphonate 

Downstream Products

• 877-95-2 methyl-N-(benzyl-methyl)-formamide 

Relevant academic research and scientific papers

Revisiting the biosynthesis of dehydrophos reveals a tRNA-dependent pathway

Bioactive natural products containing a C-P bond act as mimics of phosphate esters and carboxylic acids, thereby competing with these compounds for active sites of enzymes. Dehydrophos (DHP), a broad-spectrum antibiotic, is a phosphonotripeptide produced by Streptomyces luridus, in which glycine and leucine are linked to an aminophosphonate analog of dehydroalanine, ΔAla(P). This unique feature, in combination with the monomethylation of the phosphonic acid, renders DHP a Trojan horse type antibiotic because peptidase-mediated hydrolysis will release methyl acetylphosphonate, a potent inhibitor of pyruvate dehydrogenase. Bioinformatic analysis of the biosynthetic gene cluster suggested that ΔAla(P) would be generated from Ser(P), the phosphonate analog of Ser, by phosphorylation and subsequent elimination, and that ΔAla(P) would be condensed with Leu-tRNALeu. DhpH was anticipated to carry out this elimination/ligation cascade. DhpH is a multidomain protein, in which a pyridoxal phosphate binding domain is fused to an N-acetyltransferase domain related to the general control non-derepressible- 5 (GCN5) family. In thiswork, the activity of DhpH was reconstituted in vitro. The enzyme was able to catalyze the β-elimination reaction of pSer(P) to generate ΔAla(P), but it was unable to condense ΔAla(P) with Leu. Instead, ΔAla(P) is hydrolyzed to acetyl phosphonate, which is converted to Ala(P) by a second pyridoxal phosphate-dependent enzyme, DhpD. Ala(P) is the substrate for the condensation with Leu-tRNALeu catalyzed by the C-terminal domain of DhpH. DhpJ, a 2-oxoglutarate/Fe(II)-dependent enzyme, introduces the vinyl functionality into Leu-Ala(P) acting as a desaturase, and addition of Gly by DhpK in a Gly-tRNAGly-dependent manner completes the in vitro biosynthesis of dehydrophos.

pH-Dependent Decomposition of β-Hydroxy-Substituted Organophosphorus Complexants

Substituted ethane-1,1-diphosphonic acids containing a β-hydroxyl group undergo facile pH-dependent decomposition to phosphoric acid and acetylphophonate.The decomposition is observed in acidic medium, while the system is stable in basic solutions.

Use of the dehydrophos biosynthetic enzymes to prepare antimicrobial analogs of alaphosphin

The C-terminal domain of the dehydrophos biosynthetic enzyme DhpH (DhpH-C) catalyzes the condensation of Leu-tRNALeu with (R)-1-aminoethylphosphonate, the aminophosphonate analog of alanine called Ala(P). The product of this reaction, Leu-Ala(P), is a phosphonodipeptide, a class of compounds that have previously been investigated for use as clinical antibiotics. In this study, we show that DhpH-C is highly substrate tolerant and can condense various aminophosphonates (Gly(P), Ser(P), Val(P), 1-amino-propylphosphonate, and phenylglycine(P)) to Leu. Moreover, the enzyme is also tolerant with respect to the amino acid attached to tRNALeu. Using a mutant of leucyl tRNA synthetase that is deficient in its proofreading ability allowed the preparation of a series of aminoacyl-tRNALeu derivatives (Ile, Ala, Val, Met, norvaline, and norleucine). DhpH-C accepted these aminoacyl-tRNA derivatives and condensed the amino acid with l-Ala(P) to form the corresponding phosphonodipeptides. A subset of these peptides displayed antimicrobial activities demonstrating that the enzyme is a versatile biocatalyst for the preparation of antimicrobial peptides. We also investigated another enzyme from the dehydrophos biosynthetic pathway, the 2-oxoglutarate dependent enzyme DhpA. This enzyme oxidizes 2-hydroxyethylphosphonate to 1,2-dihydroxyethylphosphonate en route to l-Ala(P), but longer incubation results in overoxidation to 1-oxo-2-hydroxyethylphosphonate. This α-ketophosphonate was converted by the pyridoxal phosphate dependent enzyme DhpD into l-Ser(P). Thus, the dehydrophos biosynthetic enzymes can generate not only l-Ala(P) but also l-Ser(P).

Biocatalytic resolution of enantiomeric mixtures of 1-aminoethanephosphonic acid

Several fungal strains, namely Bauveria bassiana, Cuninghamella echinulata, Aspergillus fumigatus, Penicillium crustosum and Cladosporium herbarum, were used as biocatalysts to resolve racemic mixtures of 1-aminoethanephosphonic acid using L/D amino acid oxidase activity. The course of reaction was analyzed by 31P-NMR in the presence of cyclodextrin used as chiral discriminating agent. The best result (42% e.e of R-isomer) was obtained with a strain of Cuninghamella echinulata.

Chemoselective N-acylation via condensations of N-(benzoyloxy)amines and α-ketophosphonic acids under aqueous conditions

(Chemical Equation Presented) A new amide-forming reaction with N-benzoyloxyamines and α-ketophosphonic acids was investigated. A mixed solvent of t-BuOH/water (1:1) at 40°C provided the desired amide in high yield (71-96%). Both phosphonic acids (9, 12, or 13) and their disodium salts (e.g., 10) were shown to react with the respective N-benzoyloxyamines (1b and 4) in excellent yields. The phosphonic acid methyl ester monosodium salt 11 did not react under these conditions. However, compound 11 did provide the desired amide in 22% yield upon addition of 2 equiv of TFA. The N-acylation reaction is highly chemoselective for N-benzoyloxyamines as both aliphatic amines and N-hydroxylamines were shown not to react productively with the α-ketophosphonic acids under the conditions tested. Moreover, the α-ketophosphonic acids are more selective than the related α-ketocarboxylic acid systems, which react with both the N-hydroxylamines and N-benzoyloxyamines. In this regard, this novel phosphonic acid methodology provides a new high-yielding, chemoselective acylating reagent for further study.

Arylindazoles and their use as herbicides

This invention relates to substituted aryl indazoles, a process for producing them and their use as herbicides. In particular this invention relates to substituted aryl indazoles of the formula STR1 wherein all variables are as defined in the specification.

Acylphosphonic acids and methyl hydrogen acylphosphonates: Physical and chemical properties and theoretical calculations

Acylphosphonic acids (5) and methyl hydrogen acylphosphonates (3) were synthesized by di- and mono-demethylation of dimethyl acylphosphonates (1). Spectroscopic data (i.r., 31P and 1H n.m.r.) are reported for these types of compounds for the first time. Examination of their hydrolytic stability under acidic and basic conditions revealed that except for methyl hydrogen acylphosphonates (3) that are unstable under highly alkaline pH conditions, the C-P bond in these types of compounds is stable in most cases. Nucleophilic reagents, e.g. amines, borohydride, or hydroxylamine react with the carbonyl group of ionized acylphosphonates with the preservation of the C-P bond, to yield α-imino-, α-hydroxy-, or α-oxyimino- alkylphosphononate anions, respectively. Semi-empirical quantum mechanical (MNDO/H) calculations were performed on benzoylphosphonic acid (5c) and on the esters and anions derived from it, as representatives of their classes, in order to assess bond lengths and preferred conformations, and to estimate charges on the carbonyl and phosphoryl groups. Calculations show that for both neutral and ionized (anions) compounds free rotation around the C-P bond is expected due to the low energy barriers.

Alkoxycarbonylphosphonic acid derivative brush control agents

Alkoxycarbonylphosphonic acids and alkylthiocarbonylphosphonic acids and esters and salts of these acids such as diammonium methoxycarbonylphosphonate are useful for regulation of the growth rate of plants.