The latter two complexes were inactive. PD-0332991 solubility dmso The kinetic study using the LD technique showed that the cleavage of dsDNA by the Cu(bpy)2 complex consists of two first order reactions. The first is proposed to reflect the scission of one strand, whereas the slow reaction is due to the cleavage of the complementary strand near the first cleaved site. The reactive oxygen species is the oxygen radical which is produced by oxidation of the central Cu(II) ion. This study was supported by the National Research Foundation (grant nos. 2012-008875 conferred to S.K. Kim and SRC program 2011-0001335 to J. Kim).

“
“Current Opinion in Chemical Biology 2014, 19:25–33 This review comes from a themed issue on Biocatalysis and biotransformation Edited by Jeffrey C Moore and Uwe T Bornscheuer For a complete overview see the Issue and the Editorial Available online 4th January 2014 1367-5931/$ – see front matter, © 2013 The

Authors. Published by Elsevier Ltd. All rights reserved. http://dx.doi.org/10.1016/j.cbpa.2013.12.010 The formation of carbon-carbon bonds is central to organic chemistry and the aldol condensation [1, 2, 3 and 4], the reaction of two carbonyl compounds to generate a new β-hydroxyl carbonyl compound, is an important tool in building up complexity of organic molecules, IDO inhibitor since up to two new stereogenic centres are made during the formation of the new C–C bond. Aldol structural units Niclosamide are found in many naturally occurring molecules and are the result of reactions catalysed by the aldolase family of enzymes. These enzymes convert their substrates into the aldol products in high yield with high specificity under mild conditions,

but also with great control over the relative and absolute configurations of the new stereogenic centres created. These properties make aldolase-catalysed routes attractive for the production of biologically significant compounds, as these tend to contain multiple functional groups and are often water-soluble making conventional synthetic routes more difficult [5]. However, naturally occurring aldolases do not exist for many industrially important reactions and protein engineering, directed evolution and de novo enzyme design [ 6, 7, 8, 9 and 10] have all been used to alter properties such as stability, substrate specificity and stereoselectivity to produce tailor made aldolases for use as biocatalysts. Since we reviewed this area in 2008 [ 11] it is pleasing to see an increasing use of protein engineering to manipulate aldolases as new biocatalysts, both in their own right and as part of chemical cascade reactions leading to important products (see Table 1 for a summary of recent examples of engineering aldolases).