Building mutual trust: a framework project for implementing EU common standards in legal interpreting and translation

This edited volume addresses the establishment of core competencies for legal interpreters and translators(LITs) in the European common area, guides to core interpreter training curricula, the training of interpreter trainers, guidance for judicial professionals on working through legal interpreters and an extensive training materials resource bank

Comparative and Functional Genomics of Rhodococcus opacus PD630 for Biofuels Development

The Actinomycetales bacteria Rhodococcus opacus PD630 and Rhodococcus jostii RHA1 bioconvert a diverse range of organic substrates through lipid biosynthesis into large quantities of energy-rich triacylglycerols (TAGs). To describe the genetic basis of the Rhodococcus oleaginous metabolism, we sequenced and performed comparative analysis of the 9.27 Mb R. opacus PD630 genome. Metabolic-reconstruction assigned 2017 enzymatic reactions to the 8632 R. opacus PD630 genes we identified. Of these, 261 genes were implicated in the R. opacus PD630 TAGs cycle by metabolic reconstruction and gene family analysis. Rhodococcus synthesizes uncommon straight-chain odd-carbon fatty acids in high abundance and stores them as TAGs. We have identified these to be pentadecanoic, heptadecanoic, and cis-heptadecenoic acids. To identify bioconversion pathways, we screened R. opacus PD630, R. jostii RHA1, Ralstonia eutropha H16, and C. glutamicum 13032 for growth on 190 compounds. The results of the catabolic screen, phylogenetic analysis of the TAGs cycle enzymes, and metabolic product characterizations were integrated into a working model of prokaryotic oleaginy.Cambridge-MIT InstituteMassachusetts Institute of Technology. (Seed Grant program)Shell Oil CompanyNational Institute of Allergy and Infectious Diseases (U.S.)United States. National Institutes of HealthNational Institutes of Health. Department of Health and Human Services (Contract No. HHSN272200900006C

Stereoselective, Biocatalytic Reductions of α-chloro-β-keto Esters

Homochiral glycidic esters are versatile intermediates that can be converted into a variety of high-value products. Optically active glycidates can be prepared by a number of routes including asymmetric Darzens reactions, chiral alkene oxidation methodologies, and ring closure of homochiral α-halo-β-hydroxy esters (see ref 1 and references cited therein). We were particularly interested in the last strategy because asymmetric reductions of α-chloro-β-keto esters might afford each of the four possible glycidate precursors via dynamic kinetic resolution processes from single, inexpensive starting materials (Scheme 1). Here, we explore the potential of individual reductase enzymes from baker\u27s yeast (Saccharomyces cerevisiae) as solutions to the problem of obtaining homochiral glycidate precursors. Reductions of α-chloro-β-keto esters by whole cells of commercial baker\u27s yeast generally produce disappointing mixtures of alcohol diastereomers.2-5 Recent work has revealed that the yeast genome encodes a large number of reductases,6 and it seemed likely that their simultaneous participation was mainly responsible for the modest stereoselectivities commonly observed in yeast-mediated ketone reductions.7-9 In response, we have adapted a fusion protein strategy10 that allows the properties of yeast reductases to be assessed individually, so that enzymes yielding homochiral products can be uncovered.11,12 Moreover, after a reductase with the desired properties has been identified, whole Escherichia coli cells expressing the same protein can be employed for bioconversions on preparative scales using glucose fed-batch conditions.13 Cellular metabolic pathways supply NADPH and the whole cells display very high stereoselectivities because they express only a single yeast reductase

F-19 chemical shifts, coupling constants and conformational preferences in monosubstituted perfluoroparacyclophanes

Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)In the process of studying the chemistry of perfluoro[2.2]paracyclophanes (PFPCs), a novel class of compounds, it became necessary to identify some disubstituted products. To achieve this goal, we characterize in this work some monosubstituted PFPCs, identifying their F-19-F-19 coupling patterns, and establishing a methodology for the assignment of their F-19 chemical shifts. The pattern of coupling constants indicates a skewed geometry in which the upper deck moves towards or away from the substituent, depending on the substituent electron-donor character and size. Quantum chemical calculations, performed at the HF/6-311 + G(d,p)//B3LYP/EPR-III level of theory, confirmed the conformations inferred from coupling constants and reproduced well the values of the couplings. Transmission mechanisms for the FC term of four- and five-bond F-19-F-19 couplings are discussed in detail. Understanding the conformational preferences of PFPCs and how they are reflected by the coupling constants facilitates the assignment of F-19 chemical shifts in monosubstituted PFPCs and the identification of the disubstituted products. Copyright (C) 2011 John Wiley & Sons, Ltd.49393105CONICET [5119/05]UBACYT [X-047]Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)CONICET [5119/05]UBACYT [X-047]FAPESP [06/03980-2, 08/06282-0

Synthetic Strategy toward γ-Keto Nitriles and Their Biocatalytic Conversion to Asymmetric γ-Lactones

Asymmetric γ-hydroxy nitriles are valuable intermediates because hydrolysis of the nitriles can result in an intramolecular cyclization to chiral γ-lactones, which have a variety of biological uses. Starting with an assortment of different aldehydes (alkyl and aryl) a 4-step synthesis of γ-keto nitriles was developed. These prochiral substrates were then screened against a library of ketoreductases for their ability to stereoselectively reduce the carbonyl. Enzymes from the short chain dehydrogenase family showed activity and these enzymatic reactions were scaled up to produce a diverse set of chiral γ-lactones