Quinolin-8-yl Formate: A New Option for Small-Scale Carbonylation Reactions in Microwave Reactors

A convenient procedure for conducting small-scale carbonylations of aryl or benzyl halides in a microwave reactor by using quinolin-8-yl formate is described. The resulting 8-acyloxyquinolines were shown to be more reactive than phenyl esters in acyl-transfer reactions, and their utility for the production of esters and amides was demonstrated.

Evolutionary relationships of microbial transglutaminases

Transglutaminases (TGases) are a class of enzyme widely spread in nature, and observed in plants, microorganisms, vertebrates and invertebrates. This enzyme catalyzes post-translational protein modification, by acyl transfer reactions, deamidation and crosslinking (polymerisation). There is a large interest for TGases functions, in particular for human TGases and their involvement in physiopathological processes. In bacteria, TGases appear largely present, although the function of this enzyme is still unknown. Microbial TGases (MTG, or MTGase) are of extreme interest, in particular MTGase from Streptomyces mobaraensis, used in biopolymers industry, in cosmetics production, in wool textiles, and in the food processing. We present the results of bioinformatics analysis on MTGases sequences, based on database searching, sequence comparisons and alignments, phylogenetic tree constructions, with the aim of improving the knowledge of MTGases, in the perspective of investigating by protein modelling and simulations techniques the functional features.

Evolutionary relationships of microbial transglutaminases

Transglutaminases (TGases) are a class of enzyme widely spread in nature, and observed in plants, microorganisms, vertebrates and invertebrates. This enzyme catalyzes post-translational protein modification, by acyl transfer reactions, deamidation and crosslinking (polymerisation). There is a large interest for TGases functions, in particular for human TGases and their involvement in physiopathological processes. In bacteria, TGases appear largely present, although the function of this enzyme is still unknown. Microbial TGases (MTG, or MTGase) are of extreme interest, in particular MTGase from Streptomyces mobaraensis, used in biopolymers industry, in cosmetics production, in wool textiles, and in the food processing. We present the results of bioinformatics analysis on MTGases sequences, based on database searching, sequence comparisons and alignments, phylogenetic tree constructions, with the aim of improving the knowledge of MTGases, in the perspective of investigating by protein modelling and simulations techniques the functional features.