Characterization of the Active Site of Acetylcholinesterases by Application of Sterically Modified Acetylcholine Homologues

Our aim was to find steric limitations for the model of the active site of acetylcholinesterase and cho1inesterase. For thi<s purpose we used homologues of acetylcholine with hydrocarbon chains of increasing size at the cationic head. Catalysis of hydrolysis ceased for both enzymes, when the methyl groups of the cationic head of acetylcholine were substituted by three n-propyl groups. With data already documented in the literature and our additional experiments, under the same conditions, we were able to present models of the active sites for both enzymes

Green Pathways for the Enzymatic Synthesis of Furan-Based Polyesters and Polyamides

The attention towards the utilization of sustainable feedstocks for polymer synthesis has grown exponentially in recent years. One of the spotlighted monomers derived from renewable resources is 2,5-furandicarboxylic acid (FDCA), one of the most promising bio-based monomers, due to its resemblance to petroleum-based terephthalic acid. Very interesting synthetic routes using this monomer have been reported in the last two decades. Combining the use of bio-based monomers and non-toxic chemicals via enzymatic polymerizations can lead to a robust and favorable approach towards a greener technology of bio-based polymer production. In this chapter, a brief introduction to FDCA-based monomers and enzymatic polymerizations is given, particularly focusing on furan-based polymers and their polymerization. In addition, an outline of the recent developments in the field of enzymatic polymerizations is discussed. </p

Über die Konstitution des Cyanwasserstoffes

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