Publications by authors named "Francesca Ruffolo"
The energetic metabolism of cancer cells relies on a substantial commitment of pyruvate to the catalytic action of lactate-generating dehydrogenases. This coupling mainly depends on lactate dehydrogenase A (LDH-A), which is overexpressed in different types of cancers, and therefore represents an appealing therapeutic target. Taking into account that the activity of LDHs is exclusively exerted by their tetrameric forms, it was recently shown that peptides perturbing the monomers-to-tetramer assembly inhibit human LDH-A (hLDH-A).
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- Phosphonates, which contain a direct carbon-phosphorus bond, are important sources of phosphorus in certain environments, with 2-aminoethylphosphonate (AEP) being the most common.
- Many bacteria can break down AEP using a specific pathway involving the enzyme PhnW; however, this process has limitations due to PhnW's inability to handle other related compounds like -methyl AEP (MAEP).
- The study introduces a new group of FAD-dependent oxidoreductases that can efficiently convert MAEP to phosphonoacetaldehyde (PAA), thus enhancing the degradation pathways of AEP and allowing some bacteria to generate PAA without relying on PhnW.
Article Synopsis
- * Microorganisms, particularly bacteria, have developed systems to utilize phosphonates as a resource in phosphate-limited environments, with these systems varying in specificity.
- * Research has focused on understanding the evolution, regulation, and mechanisms of microbial enzymes that degrade phosphonates, with at least three distinct enzymatic pathways identified for breaking down the C-P bond. *