In nature, amino acids are found in two forms, L and D enantiomers, except for glycine which does not have a chiral center. The change of one form to the other will lead to a change in the primary structure of proteins and hence may affect the function and biological activity of proteins. Indeed, several D-amino acid-containing peptides (DAACPs) were isolated from patients with cataracts, Alzheimer's and other diseases. Additionally, significant levels of free D-amino acids were found in several diseases, reflecting the disease conditions. Studying the molecular mechanisms of the DAACPs formation and the alteration in D-amino acids metabolism will certainly assist in understanding these diseases and finding new biomarkers and drug targets. In this review, the presence of DAACPs and free D-amino acids and their links with disease development and progress are summarized. Similarly, we highlight some recent advances in analytical techniques that led to improvement in the discovery and analysis of DAACPs and D-amino acids.
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http://dx.doi.org/10.3390/biom11111716 | DOI Listing |
J Mol Evol
January 2025
Department of Plant and Soil Sciences, 311 Plant Science Building, University of Kentucky, Lexington, KY, 40546-0312, USA.
Amino acid racemases catalyze the interconversion of L- and D-amino acids, maintaining intracellular levels of both D- and L-amino acids. While alanine and glutamate racemases are widespread in bacteria, serine racemase (SerR) is predominantly found in animals. Recently, homologs of animal SerR were reported in some bacterial genomes, but their evolutionary distribution and functional roles remain poorly understood.
View Article and Find Full Text PDFAnaerobe
January 2025
Department of Anatomy and Cell Biology, University of Florida College of Medicine, Gainesville, FL 32610.
The probing of live bacteria via the incorporation of fluorescent D-amino acids (FDAAs) during peptidoglycan synthesis has been shown to be practical for visualizing both gram-positive and gram-negative bacterial species. This study demonstrates the reliability and applications of FDAA labelling for the fluorescent imaging of an obligate anaerobe.
View Article and Find Full Text PDFFoods
January 2025
Key Laboratory of South Subtropical Fruit Biology and Genetic Resource Utilization, Ministry of Agriculture and Rural Affairs, Guangdong Provincial Key Laboratory of Science and Technology Research on Fruit Tree, Institute of Fruit Tree Research, Guangdong Academy of Agricultural Sciences, Guangzhou 510640, China.
Litchi is one of the ancient fruits that originated in China, renowned for its high nutrition and rich flavor, and Xianjinfeng (XJF) stands as one of the most notable varieties in terms of its flavor. Investigating the metabolic changes in taste compounds during fruit development offers deeper insights into the formation patterns of fruit quality. In this study, we conducted extensive metabonomic research on the accumulation patterns of taste compounds (carbohydrates, organic acids, and amino acids) across three developmental stages of XJF litchi.
View Article and Find Full Text PDFCurr Top Med Chem
January 2025
Department of Chemistry, REVA University, Rukmini Knowledge Park, Kattigenahalli, Yelahanka, Bangalore-560064, Karnataka, India.
Antibiotics are a revolutionary discovery in modern medicine, enabling the successful treatment of bacterial infections that were once untreatable and deadly. Teixobactin, a "head-toside- chain" cyclodepsipeptide, shows great promise as a lead compound for developing new antibiotics to deal with multi-drug-resistant bacterial infections. The unique pharmacological profile and intriguing structural characteristics of teixobactin, including its unusual amino acid residues (three D-amino acids and L-allo-enduracididine), have drawn the attention of multiple research groups seeking to create new antibiotics with innovative mechanisms.
View Article and Find Full Text PDFBiomolecules
December 2024
Bach Institute of Biochemistry, Research Centre of Biotechnology of the Russian Academy of Sciences, Leninsky Ave. 33, bld. 2, 119071 Moscow, Russia.
The first monomeric pyridoxal-5'-phosphate (PLP)-dependent transaminase from a marine, aromatic-compound-degrading, sulfate-reducing bacterium Tol2, has been studied using structural, kinetic, and spectral methods. The monomeric organization of the transaminase was confirmed by both gel filtration and crystallography. The PLP-dependent transaminase is of the fold type IV and deaminates D-alanine and ()-phenylethylamine in half-reactions.
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