Acidic Shell Proteins of the Mediterranean Fan Mussel Pinna nobilis.

In molluscs, the shell secretion process is controlled by a set of extracellular macromolecules collectively called the shell matrix. The shell matrix, which is produced by the mantle epithelial cells during mineralization, is predominantly composed of proteins, glycoproteins, acidic polysaccharides, and chitin that precisely regulate the deposition of calcium carbonate outside the mantle cells. In the present paper, we focus on the shell of Pinna nobilis, the giant Mediterranean fan mussel, usually considered as a model for studying molluscan biomineralization processes.

Effect of substrate binding loop mutations on the structure, kinetics, and inhibition of enoyl acyl carrier protein reductase from Plasmodium falciparum.

Enoyl acyl carrier protein reductase (ENR), which catalyzes the final and rate limiting step of fatty acid elongation, has been validated as a potential drug target. Triclosan is known to be an effective inhibitor for this enzyme. We mutated the substrate binding site residue Ala372 of the ENR of Plasmodium falciparum (PfENR) to Methionine and Valine which increased the affinity of the enzyme towards triclosan to almost double, close to that of Escherichia coli ENR (EcENR) which has a Methionine at the structurally similar position of Ala372 of PfENR.