Results 221 to 230 of about 27,225 (279)

Catabolism of strigolactones by a carboxylesterase

Nature Plants, 2021
Strigolactones (SLs) are carotenoid-derived plant hormones that control shoot branching and communications between host plants and symbiotic fungi or root parasitic plants. Extensive studies have identified the key components participating in SL biosynthesis and signalling, whereas the catabolism or deactivation of endogenous SLs in planta remains ...
Enjun Xu, Liang Chai, Shiqi Zhang, Ruixue Yu, Xixi Zhang, Chongyi Xu, Yuxin Hu   +6 more
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Carboxylesterases (EC 3.1.1). Kinetic studies on carboxylesterases

Biochemistry, 1969
Kinetic 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., Horgan, Douglas J., Runnegar, Maria T. C., de Jersey, John, Webb, Edwin C., Zerner, Burt   +5 more
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Carboxylesterase Inhibitors: An Update

Current Medicinal Chemistry, 2018
Mammalian 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, Qiang, Jin, Dan-Dan, Wang, Qing-Kai, Qian, Da-Cheng, Hao, Guang-Bo, Ge, Ling, Yang   +6 more
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Human Liver Carboxylesterase. Properties and Comparison with Human Serum Carboxylesterase

The Journal of Biochemistry, 1983
Carboxylesterase 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). Amino Acid Composition of Liver Carboxylesterases

Canadian Journal of Biochemistry, 1975
The 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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Structure, function and regulation of carboxylesterases

Chemico-Biological Interactions, 2006
This 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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Carboxylesterases (EC 3.1.1.). A large-scale purification of pig liver carboxylesterase

Biochemistry, 1969
Two 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., Stoops, James K., Webb, Edwin C., Zerner, Burt   +3 more
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Characterization of inhibitors of specific carboxylesterases: Development of carboxylesterase inhibitors for translational application

Molecular Cancer Therapeutics, 2004
Abstract Carboxylesterases, expressed at high levels in human liver and intestine, are thought to detoxify xenobiotics. The anticancer prodrug 7-ethyl-10-[4-1-piperidino)-1-piperidino]carbonyloxycamptothecin (CPT-11) is also metabolized by carboxylesterases to produce the active drug 7-ethyl-10-hydroxycamptothecin.
Kyoung Jin P, Yoon, Janice L, Hyatt, Christopher L, Morton, Richard E, Lee, Philip M, Potter, Mary K, Danks   +5 more
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Carboxylesterases (EC 3.1.1). The Molecular Sizes of Chicken and Pig Liver Carboxylesterases

Canadian Journal of Biochemistry, 1975
The 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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KINETICS FOR THE INHIBITION OF CARBOXYLESTERASE BY MALAOXON

Canadian Journal of Biochemistry, 1967
Malaoxon and carboxylesterase undergo two separate but simultaneous reactions when mixed in solution. One results in the irreversible inhibition of carboxylesterase. In the other, malaoxon acts as a substrate and is hydrolyzed.This work is concerned primarily with the inhibition reaction, although direct evidence of the substrate reaction is also given.
A R, Main, W C, Dauterman
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