Dra. Daniela Gamenara, from the Enantioselective Synthesis Group of Bioactive Compounds (SECoBi) of the University of the Republic (Uruguay) is making a 4 months stay in our lab to work on the research topic "Development of synthetic processes involving aldolasas as biocatalysts for preparation of modified sugars ".
Digital.CSIC is the institutional repository of The Spanish National Research Council (CSIC). Through Digital.CSIC, the CSIC supports the international movement of open access and open communication of publicly funded research.
Digital.CSIC, with its commitment to open access as a strategy for dissemination of scientific publications, offers the possibility to increase their visibility and reach more readers, which also potentially result in a higher number of citations to jobs. It also offers the possibility of taking part in an international initiative, supported increasingly by the scientific community to facilitate scientific communication and recover to some extent control over the dissemination of their own publications.
In this interview, Dr. García-Junceda gives his opinion on the Open Access movement and their reasons to support it through their participation and collaboration with Digital.CSIC.
"4º ESO + Empresa," is an initiative of the Community of Madrid to bring the school to work environment, with the goal that young people will be better prepared for their future careers and raise possible scientific vocations. For three consecutive days, students become researchers and participate in the activities developed by scientists.
The three Science of Synthesis volumes on "Biocatalysis in Organic Synthesis" present a broad contemporary overview on the state of the art in enzymatic methods for asymmetric synthesis suitable for academics and industrial researchers working in the field of organic synthesis. The volumes were edited by leading chemists, K. Faber, W.-D. Fessner and N. Turner.
Our group has contributed with the chapter entitled Designed Enzymatic Cascades.
Aminoglycosides are especially useful for the treatment of hospital-acquired infections. The main problem for the application of these antibiotics is the presence of bacterial resistance enzymes, in particular, nucleotidyltransferases (ANTs). To understand the mechanisms that lead to antibiotic inactivation, we have performed a comprehensive experimental analysis of the 6-O- nucleotidyltransferase enzyme (ANT(6)) from Bacillus subtilis. The kinetic parameters revealed a narrow specificity of the ANT(6) for MgATP/streptomycin as substrates. The binding epitope of the streptomycin recognized by the ANT(6) is the streptidine moiety. Therefore, the use of streptidine as a “decoy acceptor” allows the recovery of the antibiotic activity of streptomyc in E. coli cells that are overexpressing the ANT(6).
