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Carboxylesterases (EC 3.1.1). Kinetic studies on carboxylesterases
Biochemistry, 1969Kinetic evidence has been obtained which is consistent with the formation of an acyl-enzyme intermediate in the hydrolysis of butyrate esters catalyzed by pig liver carboxylesterase. A study of the pig liver carboxylesterase- catalyzed hydrolysis of phenyl butyrate revealed activation by substrate and by modifiers such as benzene.
Stoops, James K. +5 more
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Carboxylesterases (EC 3.1.1). Amino Acid Composition of Liver Carboxylesterases
Canadian Journal of Biochemistry, 1975The amino acid compositions of the carboxylesterases from chicken, horse, ox, sheep, and pig livers are reported and compared. As would be expected for this homologous series, the compositions show a general similarity. However, there are some significant differences, but the degree to which particular pairs of enzymes differ is consistent with the ...
K, Scott, B, Zerner
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Thermostable Carboxylesterases from Hyperthermophiles
ChemInform, 2004AbstractFor Abstract see ChemInform Abstract in Full Text.
Atomi, H, Imanaka, T
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Carboxylesterase Inhibitors: An Update
Current Medicinal Chemistry, 2018Mammalian carboxylesterases are key serine hydrolases that catalyze the hydrolysis of a wide variety of ester compounds in the corresponding carboxylic acids and alcohols. In human, two major carboxylesterases, CES1 and CES2, have been identified and well-studied over the past decade.
Li-Wei, Zou +6 more
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Human Liver Carboxylesterase. Properties and Comparison with Human Serum Carboxylesterase
The Journal of Biochemistry, 1983Carboxylesterase was obtained from human liver in an electrophoretically homogeneous form. The monomeric molecular weight of the enzyme was 60,000 and the enzyme associated to form trimers. Purified human liver carboxylesterase was compared with human serum carboxylesterase, purified earlier.
T, Tsujita, H, Okuda
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Carboxylesterases (EC 3.1.1.). A large-scale purification of pig liver carboxylesterase
Biochemistry, 1969Two procedures for the large-scale purification of pig liver carboxylesterase are described. They start from chloroform-acetone powders of minced pig liver and involve ammonium sulfate fractionation, chromatography on CM-cellulose and CM-Sephadex, and gel filtration. These procedures produce an enzyme of hitherto unobtained purity.
Horgan, Douglas J. +3 more
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Enzymatic Activity of Human Carboxylesterases
Current Protocols in Toxicology, 2007AbstractThe carboxylesterases (CEs) are hydrolytic enzymes that metabolize xenobiotics that contain ester, thioester, or amide bonds. CEs are ubiquitously expressed but are found in highest concentration in membrane‐enriched fractions of the liver. This unit describes assays used to measure the enzymatic activity and tissue distribution of human CEs ...
Matthew K, Ross, Abdolsamad, Borazjani
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Carboxylesterases (EC 3.1.1). The Molecular Sizes of Chicken and Pig Liver Carboxylesterases
Canadian Journal of Biochemistry, 1975The molecular size of pig liver carboxylesterase has been investigated under a variety of conditions of pH and ionic strength. From equilibrium and velocity sedimentation at pH 4.0 and pH 7.5, and from chromatography on Sephadex G-200, we conclude that the monomeric molecular weight is ~65 000 daltons and that the enzyme associates to form trimers ...
P A, Inkerman, D J, Winzor, B, Zerner
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Structure, function and regulation of carboxylesterases
Chemico-Biological Interactions, 2006This review covers current developments in molecular-based studies of the structure and function of carboxylesterases. To allay the confusion of the classic classification of carboxylesterase isozymes, we have proposed a novel nomenclature and classification of mammalian carboxylesterases on the basis of molecular properties. In addition, mechanisms of
Tetsuo, Satoh, Masakiyo, Hosokawa
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[45] Carboxylesterases-amidases
1981Publisher Summary This chapter presents the simultaneous purification of five of the most prominent rat liver carboxylesterases-amidases. All of these enzymes are found in microsomal fraction. As a side product of the procedure described in the chapter , a dipeptidyl aminopeptidase is obtained that also belongs to the group of serine hydrolases.
Eberhard Heymann, Rolf Mentlein
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