Abstract-The growing demand for enantiomerically pure pharmaceuticals has impelled research on enzymes as catalysts for asymmetric synthetic transformations. However, the use of enzymes for this purpose was rather limited until the discovery that enzymes can work in organic solvents. Since the advent of the PCR the number of available enzymes has been growing rapidly and the tailor-made biocatalysts are becoming a reality. Thus, it has been possible the use of enzymes for the synthesis of new innovative medicines such as carbohydrates and their incorporation to modern methods for drug development, such as combinatorial chemistry. Finally, the genomic research is allowing the manipulation of whole genomes opening the door to the combinatorial biosynthesis of compounds. In this review, our intention is to highlight the main landmarks that have led to transfer the chemical efficiency shown by the enzymes in the cell to the synthesis of bioactive molecules in the lab during the last 20 years.

A multienzyme system composed by recombinant dihydroxyacetone kinase from Citrobacter freundii, fuculose-1-phosphate aldolase and acetate kinase, allows a practical one-pot C-C bond formation catalysed by dihydroxyacetone phosphate-dependent aldolases from dihydroxyacetone and an aldehyde.

Proteoglycans (PGs), including heparan sulfate forms, are important regulators of tumor progression. In the PGs biosynthetic process, the core protein is synthesized on a ribosomal template and the sugar chains are assembled post-translationally, one sugar at a time, starting with the linkage of xylose to a serine residue of the core protein and followed by galactosidation of the xylosylprotein. Hydrophobic xylopyranosides have been previously shown to prime heparan sulfate synthesis, a property that was required to cause growth inhibition of tumor cells. To know if the antiproliferative activity of synthetic xylopyranosides is related to their ability to act as "decoy acceptors" of xylosylprotein 4-β-galactosyltransferase, we have heterologously expressed the catalytic domain of the human β-1,4-GalT 7 and studied the ability of a variety of synthetic xylopyranoside derivatives to act as substrates or inhibitors of the recombinant enzyme.

Introduction: The intra-aortic balloon pump (IABP) is used to prevent complications after coronary artery bypass grafting (CABG) surgery, although some results are controversial and basal ventricular function may play a role. This study assessed the benefit of preoperative use of IABP, as stratified by the ventricular function, in a population submitted to high-surgical-risk CABG. Methods: Patients > 18 years old, with multiple coronary artery disease and thus candidates for CABG, were included. Cardiogenic shock, acute myocardial infarction (AMI), acute ventricle mechanical dysfunction, severe aortic regurgitation, tachyarrhythmia, massive pulmonary embolism, coagulopathy, or low life expectancy Escutia-Cuevas et al.

Organo-phosphorus compounds S 0080Multienzyme System for Dihydroxyacetone Phosphate-Dependent Aldolase Catalyzed C-C Bond Formation from Dihydroxyacetone. -A multienzyme system composed by recombinant dihydroxyacetone kinase from Citrobacter freundii, fuculose-1-phosphate aldolase and acetate kinase, allows a practical one-pot C-C bond formation catalyzed by dihydroxyacetone-dependent aldolases from dihydroxyacetone (I) and an aliphatic aldehyde (II). -(SANCHEZ-MORENO, I.; GARCIA-GARCIA, J. F.; BASTIDA, A.; GARCIA-JUNCEDA*, E.; Chem.