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Chemical Compound Review

SureCN76724     4-nitrophenolate

Synonyms: CHEBI:57917, ZINC12358750, AC1LD8TL, 14609-74-6, NCGC00248076-01, ...
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Disease relevance of Paranitrophenol

  • The polymer-hydrolyzing activity, but not the p-nitrophenylate esterase activity, was inhibited by complex media such as Luria-Bertani medium and by soluble E. coli proteins [1].

High impact information on Paranitrophenol

  • Burst experiments at high pH (9.1 or 8.1 for reduced or oxidized PAP, respectively), where hydrolysis of a phosphoenzyme intermediate is expected to be rate-limiting, show clear evidence for stoichiometric bursts of p-nitrophenolate from PNPP [2].
  • Previously, the metal complex of the diester methyl-p-nitrophenyl phosphate was found to hydrolyze via a two-step addition-elimination mechanism, in contrast to the concerted hydrolysis mechanism followed by uncomplexed diesters with the p-nitrophenolate leaving group [3].
  • In stopped-flow studies using p-nitrophenyl phosphate (pNPP) as a substrate, a burst of p-nitrophenolate in the full length enzyme was not observed; however, a 50-70% stoichiometric burst was observed with the PTPase domain [4].
  • 1. p-Nitrophenyl (PNP) acetate and propionate show a burst of p-nitrophenoxide release when their hydrolysis is catalysed by sheep liver cytosolic aldehyde dehydrogenase [5].
  • Rapid acetylation of the protein accompanies and largely accounts for the easily observed rapid formation of of p-nitrophenolate ion [6].

Biological context of Paranitrophenol


Associations of Paranitrophenol with other chemical compounds

  • The three inositols and their intermediate conduritols (conduramines) were tested against several glycosidases (alpha- and beta-glucosidase, alpha- and beta-galactosidase, alpha- and beta-mannosidase) in an assay that measured the rate of hydrolysis of p-nitrophenolglycosides rather than the concentration of p-nitrophenolate [9].
  • With PNP dimethylcarbamate the enzyme catalyses the slow release of approx. 1 molecule of p-nitrophenoxide per tetrameric enzyme molecule; during the reaction the enzyme becomes effectively inactivated, as the rate of hydrolysis of the acyl-enzyme is virtually zero [10].
  • When the polymerase reactions were performed in the presence of alkaline phosphatase, which digests the p-nitrophenylpyrophosphate side-product of phosphoryl transfer to the chromogenic p-nitrophenylate, an increase in absorbence at 405 nm was observed [11].
  • 4. The mitochondrial enzyme shows a low amplitude (22%) burst in the production of 4-nitrophenoxide ion during the hydrolysis of 4-nitrophenyl acetate at pH 7 [12].
  • Magnetic circular dichroism (MCD) spectra were observed to characterize the nature of the visible bands for high-spin Fe(III) protoheme derivatives with p-nitrothiophenolate, p-nitrophenolate, and methoxy anion as the fifth ligands in several solvents [13].

Gene context of Paranitrophenol

  • Mean basal PTP activities, were found to be significantly higher in diabetics than in normal subjects (type 1 diabetics: 0.36 +/- 0.01 vs 0.28 +/- 0.01 mmol p-nitrophenolate/h per g hemoglobin (Hb), P < 0.001; type 2 diabetics: 0.35 +/- 0.01 vs 0.28 +/- 0.01 mmol p-nitrophenolate/h per g Hb, P < 0.001) [14].
  • Non-steady-state kinetic studies reveal that the SN2 reaction between p-nitrophenoxide ion and methyl iodide in acetonitrile containing water follows a 2-step mechanism involving the formation of a kinetically significant intermediate [15].

Analytical, diagnostic and therapeutic context of Paranitrophenol

  • An improved assay for N-acetyl-beta-D-glucosaminidase activity in urine is described that involves (a) gel filtration to separate the enzyme from inhibitors in urine, (b) enzymic hydrolysis of p-nitrophenyl-N-acetyl-beta-D-glucosaminide at pH 4.4, and (c) spectrophotometry of the liberated p-nitrophenylate [16].
  • During the kinetic study of the destruction process, the determination of remaining concentrations of the alkylating agents was performed by the derivatization of p-nitrophenoxide to p-nitroanisole and p-nitrophenetole, which were separated by high performance liquid chromatography [17].


  1. Cloning and characterization of the poly(hydroxyalkanoic acid)-depolymerase gene locus, phaZ1, of Pseudomonas lemoignei and its gene product. Jendrossek, D., Müller, B., Schlegel, H.G. Eur. J. Biochem. (1993) [Pubmed]
  2. Evidence for a phosphoryl-enzyme intermediate in phosphate ester hydrolysis by purple acid phosphatase from bovine spleen. Vincent, J.B., Crowder, M.W., Averill, B.A. J. Biol. Chem. (1991) [Pubmed]
  3. Altered mechanisms of reactions of phosphate esters bridging a dinuclear metal center. Humphry, T., Forconi, M., Williams, N.H., Hengge, A.C. J. Am. Chem. Soc. (2004) [Pubmed]
  4. Mechanistic studies on full length and the catalytic domain of the tandem SH2 domain-containing protein tyrosine phosphatase: analysis of phosphoenzyme levels and Vmax stimulatory effects of glycerol and of a phosphotyrosyl peptide ligand. Wang, J., Walsh, C.T. Biochemistry (1997) [Pubmed]
  5. A comparison of nitrophenyl esters and lactones as substrates of cytosolic aldehyde dehydrogenase. Kitson, T.M., Kitson, K.E. Biochem. J. (1996) [Pubmed]
  6. Acetylation of human serum albumin by p-nitrophenyl acetate. Means, G.E., Bender, M.L. Biochemistry (1975) [Pubmed]
  7. A continuous spectrophotometric assay for P450 BM-3, a fatty acid hydroxylating enzyme, and its mutant F87A. Schwaneberg, U., Schmidt-Dannert, C., Schmitt, J., Schmid, R.D. Anal. Biochem. (1999) [Pubmed]
  8. Half-of-the-sites reactivity of outer-membrane phospholipase A against an active-site-directed inhibitor. Ubarretxena-Belandia, I., Cox, R.C., Dijkman, R., Egmond, M.R., Verheij, H.M., Dekker, N. Eur. J. Biochem. (1999) [Pubmed]
  9. Synthesis, structure, and biological evaluation of novel N- and O-linked diinositols. Paul, B.J., Willis, J., Martinot, T.A., Ghiviriga, I., Abboud, K.A., Hudlicky, T. J. Am. Chem. Soc. (2002) [Pubmed]
  10. The action of cytoplasmic aldehyde dehydrogenase on methyl p-nitrophenyl carbonate and p-nitrophenyl dimethylcarbamate. Kitson, T.M. Biochem. J. (1989) [Pubmed]
  11. Exploiting polymerase promiscuity: A simple colorimetric RNA polymerase assay. Vassiliou, W., Epp, J.B., Wang, B.B., Del Vecchio, A.M., Widlanski, T., Kao, C.C. Virology (2000) [Pubmed]
  12. A reinvestigation of the purity, isoelectric points and some kinetic properties of the aldehyde dehydrogenases from sheep liver. Agnew, K.E., Bennett, A.F., Crow, K.E., Greenway, R.M., Blackwell, L.F., Buckley, P.D. Eur. J. Biochem. (1981) [Pubmed]
  13. Solvent effect on MCD of Fe(III) heme complexes: magnetic circular dichroism spectra of five-coordinated high-spin iron(III) protoporphyrin-IX-dimethylester in the visible region and their environmental effect. A characterization of the visible electronic transitions in Fe(III) high-spin porphyrins. Ookubo, S., Nozawa, T., Hatano, M. J. Inorg. Biochem. (1989) [Pubmed]
  14. Insulin and high glucose modulation of phosphatase and reductase enzymes in the human erythrocytes: a comparative analysis in normal and diabetic states. Marques, F., Crespo, M.E., Silva, Z.I., Bicho, M. Diabetes Res. Clin. Pract. (2000) [Pubmed]
  15. Non-steady-state kinetic study of the SN2 reaction between p-nitrophenoxide ion and methyl iodide in aprotic solvents containing water. Evidence for a 2-step mechanism. Lu, Y., Handoo, K.L., Parker, V.D. Org. Biomol. Chem. (2003) [Pubmed]
  16. Spectrophotometric assay for urinary N-acetyl-beta-D-glucosaminidase activity. Horak, E., Hopfer, S.M., Sunderman, F.W. Clin. Chem. (1981) [Pubmed]
  17. Evaluation of methods for destruction of some alkylating agents. De Méo, M., Laget, M., Castegnaro, M., Duménil, G. American Industrial Hygiene Association journal. (1990) [Pubmed]
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