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Gene Review

CES1  -  carboxylesterase 1

Sus scrofa

Synonyms: APLE, PMPMEase, REH, TGH
 
 
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Disease relevance of CES3

  • Effect of endogenous carboxylesterase on HI-6 protection against soman toxicity [1].
 

High impact information on CES3

  • In contrast, nitrosamide and nitrosocarbamate stability, mutagenicity, and DNA cross-linking activity were rapidly decreased in the presence of plasma or carboxylesterase [2].
  • The effects of mouse plasma, human plasma, and purified porcine liver carboxylesterase on nitrosourea, nitrosamide, and nitrosocarbamate chemical stability, mutagenicity, and DNA cross-linking activity were compared [2].
  • This study provides insight into the mechanism of carboxylesterase inhibition and raises the possibility that inhibitors that too strongly favor the gem-diol configuration have decreased potency due to low rate of ketone formation [3].
  • The amino acid promoiety and the esterification site influenced carboxylesterase hydrolysis rates up to 1164-fold and the binding affinity up to 26-fold [4].
  • Nucleoside ester prodrug substrate specificity of liver carboxylesterase [4].
 

Biological context of CES3

 

Anatomical context of CES3

 

Associations of CES3 with chemical compounds

 

Analytical, diagnostic and therapeutic context of CES3

References

  1. Effect of endogenous carboxylesterase on HI-6 protection against soman toxicity. Maxwell, D.M., Koplovitz, I. J. Pharmacol. Exp. Ther. (1990) [Pubmed]
  2. Effect of plasma and carboxylesterase on the stability, mutagenicity, and DNA cross-linking activity of some direct-acting N-nitroso compounds. Aukerman, S.L., Brundrett, R.B., Hilton, J., Hartman, P.E. Cancer Res. (1983) [Pubmed]
  3. Use of ab initio calculations to predict the biological potency of carboxylesterase inhibitors. Wheelock, C.E., Colvin, M.E., Uemura, I., Olmstead, M.M., Sanborn, J.R., Nakagawa, Y., Jones, A.D., Hammock, B.D. J. Med. Chem. (2002) [Pubmed]
  4. Nucleoside ester prodrug substrate specificity of liver carboxylesterase. Landowski, C.P., Lorenzi, P.L., Song, X., Amidon, G.L. J. Pharmacol. Exp. Ther. (2006) [Pubmed]
  5. Purification and molecular cloning of porcine intestinal glycerol-ester hydrolase--evidence for its identity with carboxylesterase. David, L., Guo, X.J., Villard, C., Moulin, A., Puigserver, A. Eur. J. Biochem. (1998) [Pubmed]
  6. Enhancement of hepatic microsomal esterase activity following soman pretreatment in guinea pigs. Luttrell, W.E., Castle, M.C. Biochem. Pharmacol. (1993) [Pubmed]
  7. Myristyl and palmityl acylation of pI 5.1 carboxylesterase from porcine intestine and liver. Smialowski-Fléter, S., Moulin, A., Perrier, J., Puigserver, A. Eur. J. Biochem. (2002) [Pubmed]
  8. Monoclonal antibodies distinguish between carboxylesterase isoenzymes in different tissues of rat and guinea pig. Gaustad, R., Løvhaug, D. Biochem. Pharmacol. (1992) [Pubmed]
  9. Substituted trifluoroketones as potent, selective inhibitors of mammalian carboxylesterases. Ashour, M.B., Hammock, B.D. Biochem. Pharmacol. (1987) [Pubmed]
  10. The equivalent weight of pig liver carboxylesterase (EC 3.1.1.1) and the esterase content of microsomes. Kunert, M., Heymann, E. FEBS Lett. (1975) [Pubmed]
  11. Transport, uptake, and metabolism of the bis(pivaloyloxymethyl)-ester prodrug of 9-(2-phosphonylmethoxyethyl)adenine in an in vitro cell culture system of the intestinal mucosa (Caco-2). Annaert, P., Kinget, R., Naesens, L., de Clercq, E., Augustijns, P. Pharm. Res. (1997) [Pubmed]
  12. Carboxylesterases in guinea pig. A comparison of the different isoenzymes with regard to inhibition by organophosphorus compounds in vivo and in vitro. Gaustad, R., Johnsen, H., Fonnum, F. Biochem. Pharmacol. (1991) [Pubmed]
  13. Slow-binding inhibition of carboxylesterase and other serine hydrolases by chlorodifluoroacetaldehyde. Yin, H., Jones, J.P., Anders, M.W. Chem. Res. Toxicol. (1993) [Pubmed]
  14. Recombinant porcine intestinal carboxylesterase: cloning from the pig liver esterase gene by site-directed mutagenesis, functional expression and characterization. Musidlowska-Persson, A., Bornscheuer, U.T. Protein Eng. (2003) [Pubmed]
 
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