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Carboxylesterases (CES) are a superfamily of serine hydrolases present in all kingdoms of life. Human CES2 is a serine hydrolase that is recruited to the plasma membrane during efflux of cytotoxic or toxic xenobiotics and xenobiotics that are anti-inflammatory or anti-thrombotic. There is no crystal structure of a functional CES2. To understand the molecular basis of the catalytic activity of CES2, CES2 was purified from a human placenta cDNA library. After screening a series of conditions, CES2 was purified using an affinity column containing aldehyde-modified bovine serum albumin. CES2 purified from human placental membranes was a dimer of identical subunits of relative mass 66kDa on native PAGE and 75kDa after reduction of the disulfide bonds. The N-terminal sequence was derived from a partially purified protein by Edman degradation, which also contained CES1. The disulfide bonds were confirmed by mass spectrometry. Benzyl acetate was used as a model substrate to show the hydrolysis of non-natural substrates by the enzyme. Benzyl esters were hydrolyzed more rapidly than the corresponding alkyl esters. The kinetic constants determined with the benzyl esters showed a similar K(m) to p-nitrophenyl acetate.In major depressive episodes, the release of inflammatory cytokines such as tumor necrosis factor-alpha is associated with the clinical symptoms.
In major depressive disorder (MDD), anti-depressants are used to treat depression but no effective medical therapies have been developed. The effect of anti-depressants
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