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Chemical Compound Review

PNP-ACETATE     (4-nitrophenyl) ethanoate

Synonyms: CHEMBL40988, SureCN74985, NSC-2633, AG-H-31783, ACMC-209pqz, ...
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Disease relevance of NSC 2633

  • The purified lipase from Pseudomonas cepacia was used as free and immobilized enzyme preparation for hydrolysis of p-nitrophenyl palmitate (pNPP) and p-nitrophenyl acetate (pNPA) in organic media [1].

High impact information on NSC 2633

  • The most stable esterase, 8G8, has 13 amino acid substitutions, a melting temperature 17 degrees C higher than the wild-type enzyme, and increased hydrolytic activity toward p-nitrophenyl acetate (pNPA), the substrate used for evolution, at all temperatures [2].
  • The kcat/KM for PNPA hydrolysis and KOCN are linearly dependent on the hydrophobicity of the amino acid at position 143 [3].
  • The values of kcat/Km for the reactions of four substrates, p-nitrophenyl acetate (PNPA), propionyl-beta-methylthiocholine (PrMSCh), 3,3-dimethylbutyl thioacetate (DBTA), and acetylthiocholine (AcSCh), with acetylcholinesterase were determined as a function of increasing viscosity (eta rel) in sucrose-containing and in glycerol-containing buffers [4].
  • Solvent deuterium isotope effects on the rates of lipoprotein lipase (LpL) catalyzed hydrolysis of the water-soluble esters p-nitrophenyl acetate (PNPA) and p-nitrophenyl butyrate (PNPB) have been measured and fall in the range 1.5-2 [5].
  • The effect of apolipoprotein C-II (apoC-II) on the LpL-catalyzed hydrolysis of PNPA and PNPB has been determined [6].

Biological context of NSC 2633

  • CONCLUSIONS: Determination of patient plasma pNPA hydrolysis activity may have utility in predicting SN-38 pharmacokinetics during prolonged infusions of irinotecan [7].

Anatomical context of NSC 2633

  • The PNPA tests confirmed that HE proteins of EBCV and RBCV were functionally expressed in transfected COS-7 cells [8].

Associations of NSC 2633 with other chemical compounds

  • KI values for apoC-II inhibition of the LpL-catalyzed hydrolysis of PNPA and PNPB are in the range 0.26-0.83 microM [6].
  • 2. The administration of PFDA rather specifically decreases PNPA hydrolase activity and RL1 content [9].
  • The rate constant of pNPA hydrolysis catalyzed by alpha-CHT of the activated pathway kA by halothane was 0.269 s-1, whereas that of the normal pathway was k0 0.093 s-1 [10].
  • In order to explore these abilities, the reactions involving hydrolysis of p-nitrophenyl acetate (PNPA) and transesterification of PNPA with n-butanol were chosen [11].

Gene context of NSC 2633

  • One assay used p-nitrophenyl acetate (PNPA) as substrate and detected serine-esterase activity; the second assay monitored AE function with bovine submaxillary mucin (BSM) as substrate [8].

Analytical, diagnostic and therapeutic context of NSC 2633

  • The specific activity of the lipase was greatly enhanced upon immobilization: 16.5- and 7.8-fold for pNPP and pNPA respectively [1].


  1. Activity of Pseudomonas cepacia lipase in organic media is greatly enhanced after immobilization on a polypropylene support. Pencreac'h, G., Baratti, J.C. Appl. Microbiol. Biotechnol. (1997) [Pubmed]
  2. Tryptophan phosphorescence study of enzyme flexibility and unfolding in laboratory-evolved thermostable esterases. Gershenson, A., Schauerte, J.A., Giver, L., Arnold, F.H. Biochemistry (2000) [Pubmed]
  3. Functional consequences of engineering the hydrophobic pocket of carbonic anhydrase II. Fierke, C.A., Calderone, T.L., Krebs, J.F. Biochemistry (1991) [Pubmed]
  4. Fractional diffusion-limited component of reactions catalyzed by acetylcholinesterase. Bazelyansky, M., Robey, E., Kirsch, J.F. Biochemistry (1986) [Pubmed]
  5. Solvent isotope effects for lipoprotein lipase catalyzed hydrolysis of water-soluble p-nitrophenyl esters. Quinn, D.M. Biochemistry (1985) [Pubmed]
  6. Lipoprotein lipase catalyzed hydrolysis of water-soluble p-nitrophenyl esters. Inhibition by apolipoprotein C-II. Quinn, D.M., Shirai, K., Jackson, R.L., Harmony, J.A. Biochemistry (1982) [Pubmed]
  7. Human plasma carboxylesterase and butyrylcholinesterase enzyme activity: correlations with SN-38 pharmacokinetics during a prolonged infusion of irinotecan. Guemei, A.A., Cottrell, J., Band, R., Hehman, H., Prudhomme, M., Pavlov, M.V., Grem, J.L., Ismail, A.S., Bowen, D., Taylor, R.E., Takimoto, C.H. Cancer Chemother. Pharmacol. (2001) [Pubmed]
  8. Temperature-sensitive acetylesterase activity of haemagglutinin-esterase specified by respiratory bovine coronaviruses. Lin, X.Q., Chouljenko, V.N., Kousoulas, K.G., Storz, J. J. Med. Microbiol. (2000) [Pubmed]
  9. Differences in the induction of carboxylesterase isozymes in rat liver microsomes by perfluorinated fatty acids. Hosokawa, M., Satoh, T. Xenobiotica (1993) [Pubmed]
  10. Volatile anesthetics-induced activation phenomena of alpha-chymotrypsin-catalyzed hydrolysis. Seto, T., Makimoto, S., Mashimo, T., Yoshiya, I., Taniguchi, Y. Biochim. Biophys. Acta (1992) [Pubmed]
  11. Immobilization of lipases and assay in continuous fixed bed reactor. dos Reis-Costa, L., Soares, A.M., França, S.C., Trevisan, H.C., Roberts, T.J. Protein Pept. Lett. (2003) [Pubmed]
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