Publications by authors named "Tamara Dinhof"
Article Synopsis
- 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. *
α-Aminophosphonic acids have a remarkably broad bioactivity spectrum. They can function as highly efficient transition state mimics for a variety of hydrolytic and angiotensin-converting enzymes, which makes them interesting target structures for synthetic chemists. In particular, the phosphonic acid analogs to α-aminocarboxylic acids (P AAs) are potent enzyme inhibitors, but many of them are only available by chiral or enzymatic resolution; sometimes only one enantiomer is accessible, and several have never been prepared in enantiopure form at all.
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