D-amino-acid dehydrogenase (EC 1.4.99.1) is a bacterial enzyme that catalyses the oxidation of D-amino acids into their corresponding oxoacids.
[4] D-amino acids are used as components of pharmaceutical products, such as antibiotics, anticoagulants, and pesticides, because they have been shown to be not only more potent than their L enantiomers, but also more resistant to enzyme degradation.
[5] Solubilized D-amino acid dehydrogenase tends to increase its affinity for D-alanine, D-asparagine, and D-
[10] In one study, in order to test the viability of using D-amino dehydrogenase in synthesis reactions, researchers used mutant bacteria to obtain and create different strains of the enzyme.
They also found that it retained its highly selective nature, capable of receiving mostly D-enantiomers after mutation, with yields in excess of 95%.
[11] From the given studies, in order to obtain D-amino acid dehydrogenase one must first introduce and express it within a given bacterial species, some of which have been previously referenced.
For example, it was found that specifically D-alanine dehydrogenases from E. coli and P. aeruginosa would lose most of their activity when subjected to conditions of 37 - 42 °C.