Disease relevance of NSC 1552

• Pseudomonas putida B2 is able to grow on o-nitrophenol (ONP) as the sole source of carbon and nitrogen [1].
• Detection of virulence factors in culturable Escherichia coli isolates from water samples by DNA probes and recovery of toxin-bearing strains in minimal o-nitrophenol-beta-D-galactopyranoside-4-methylumbelliferyl-beta-D-g luc uronide media [2].
• With a model system (coculture of Pseudomonas putida B2 and Sphingomonas stygia incubated with [14C] o-nitrophenol), combination of MAR and FISH was shown to be able to successfully identify the microorganisms degrading o-nitrophenol [3].
• Anaerobic Toxicity Assay (ATA) tests were conducted on acidogenic cultures to assess the feasibility of using acidogenic processes to treat wastewaters containing 2-nitrophenol [4].

High impact information on NSC 1552

• Absorption spectra indicate that the fields around 2-nitrophenol of 6a-c situated in liposome membranes are more hydrophobic than that of 9 in an aqueous solution, whereas the environments around deprotonated 2-nitrophenolate of 6b and 6c are not so hydrophobic as that of 6a [5].
• Absorption spectra and (1)H NMR spectra respectively suggest that protonated 2-nitrophenol groups of 6a and those of 6c might take face-to-face associations in bilayer membranes [5].
• The transfection efficiency was determined with the fluorometric ONPG (o-nitrophenol-beta-D-galactopyranoside) assay and histochemical X-gal staining [6].
• The PATS is an active transport system that is strongly inhibited by 2,4-dinitrophenol, 4-nitrophenol (100%), KCN (97%), 2-nitrophenol (90%), or NaN3 (80%) added at a 1 mM final concentration (each) [7].
• At various time points postadministration, the animals were sacrificed and transgene expression in the tumor and liver was determined quantitatively by the ONPG to ONP enzymatic conversion assay and qualitatively by X-gal staining [8].

Chemical compound and disease context of NSC 1552

• Salicylate hydroxylase [EC 1.14.13.1] from Pseudomonas putida catalyzes the hydroxylation of salicylate, and also o-aminophenol, o-nitrophenol, and o-halogenophenols, to catechol [9].

Biological context of NSC 1552

• The beta-galactosidase-catalyzed hydrolysis of o-nitrophenol-beta-D-galactoside at subzero temperatures: evidence for a galactosyl-enzyme intermediate [10].
• The fact that one atom of 18O2 was incorporated into the produced catechol in hydroxylation of o-nitrophenol indicates that the reaction is of monooxygenase nature [11].
• The effect of COD/NO(3)(-)-N ratio on the biotransformation and removal of 2-nitrophenol (2-NP), 4-nitrophenol (4-NP), and 2,4-dinitrophenol (2,4-DNP) was studied in bench scale upflow anaerobic sludge blanket (UASB) reactors [12].

Anatomical context of NSC 1552

• Deprotonated 2-nitrophenol groups of 6b and 6c must be located in less hydrophobic circumstances, while that of 6a is still embedded in bilayer membranes because of its larger hydrophobicity [5].
• RESULTS: An O-demethylated metabolite of 2-NA, 2-nitrophenol (2-NP), and two oxidation products of this metabolite [2,5-dihydroxynitrobenzene (2,5-DNB) and 2,6-dihydroxynitrobenzene (2,6-DNB)] were generated by microsomes and P450s from the species investigated, but at different levels [13].

Associations of NSC 1552 with other chemical compounds

• The sensing scheme was based on the decrease of yellow product, o-nitrophenol, from a colorless substrate, o-nitrophenyl acetate, due to the inhibition by organophosphorus compounds on AChE [14].
• Photomineralization of 2-nitrophenol in aqueous medium was investigated as a function of the following experimental parameters: initial concentration of pollutant, light intensity, initial concentration of hydroperoxide, catalyst concentration, pH and temperature [15].
• In an effort to develop novel prodrugs for viral directed enzyme prodrug therapy (VDEPT) approaches to chemotherapy, eleven esters and carbamates of o-nitrophenol, p-nitrophenol, and beta-naphthol were synthesized and characterized as substrates for rabbit (rCE) and human liver (hCE1) carboxylesterases [16].
• The well-known beta-gal substrate analog, o-nitrophenyl beta-d-galactopyranoside, yields the visibly colored, o-nitrophenol product upon hydrolysis, whereas the substrate, p-aminophenyl beta-D-galactopyranoside, gives rise to an electrooxidizable product, p-aminophenol [17].
• 2-aminophenol was identified as the major metabolite of the biotransformation of 2-nitrophenol [4].

Gene context of NSC 1552

• Hydroxylation of o-halogenophenol and o-nitrophenol by salicylate hydroxylase [11].

References