Enzymatic Synthesis of Biologically Active -Phosphinic Analogue of α-Ketoglutarate.

Amino acid analogues with a phosphorus-containing moiety replacing the carboxylic group are promising sources of biologically active compounds. The -phosphinic group, with hydrogen-phosphorus-carbon (H-P-C) bonds and a flattened tetrahedral configuration, is a bioisostere of the carboxylic group. Consequently, amino--phosphinic acids undergo substrate-like enzymatic transformations, leading to new biologically active metabolites.

Revealing O-acetylhomoserine sulfhydrylase involved in direct sulfhydrylation pathway in Clostridium tetani.

Bacterial methionine biosynthesis is an attractive target for research due to its central role in cellular metabolism, as most steps of this pathway are missing in mammals. Up to now little is known about sulfur metabolism in pathogenic Clostridia species, making the study of the enzymes of Cys/Met metabolism in Clostridium tetani particularly relevant. Analysis of the C.

The concept of Gallium-controlled double C-H functionalization of aliphatic CH-groups driven by Vinyl carbocations.

The direct C-H activation of inert C(sp)-H bonds in a hydrocarbon chain has been a very attractive target in organic synthesis for many decades. Among all the variety of processes, those driven by vinyl carbocations are quite scarce thus far, and it is hard to control for unstabilized vinyl cations. In this study, we designed a double C(sp)-H functionalization of unactivated alkyl CH groups to produce a totally substituted quaternary carbon stereocenter via insertion of vinyl carbocations.

Anticandidal Activity of In Situ Methionine γ-Lyase-Based Thiosulfinate Generation System vs. Synthetic Thiosulfinates.

and non-albicans species are a common cause of human mucosal infections, as well as bloodstream infections and deep mycoses. The emergence of resistance of spp. to antifungal drugs used in practice requires the search for new antimycotics.

Hemoglobin is an oxygen-dependent glutathione buffer adapting the intracellular reduced glutathione levels to oxygen availability.

Fast changes in environmental oxygen availability translate into shifts in mitochondrial free radical production. An increase in intraerythrocytic reduced glutathione (GSH) during deoxygenation would support the detoxification of exogenous oxidants released into the circulation from hypoxic peripheral tissues. Although reported, the mechanism behind this acute oxygen-dependent regulation of GSH in red blood cells remains unknown.