D-Serine-Dehydratase from Saccaromyces cerevisiae: A Pyridoxal 5’- phosphate-Dependent Enzyme for Advanced Biotech Applications

Abstract

The Saccaromices cerevisiae D-serine dehydratase is a pyridoxal 5'-phosphate dependent enzyme that requires zinc for its function. It catalyses the conversion of D-serine into pyruvate and ammonia with the K(m) and k(cat) values of 0.39 mM and 13.1 s(-1) respectively. In this work, a new methodology for monitoring D-serine is presented. Our results show that this enzyme could be successfully used as a biological probe for detection of D-serine via fluorescence spectroscopy.

Biosensors for D-Amino Acids: Detection Methods and Applications

“…An earlier chemiluminescence flow biosensor was developed using a column with immobilized pkDAAO onto amine-modified silica gel: hydrogen peroxide produced by the enzymatic reaction on total D-AAs was reacted with luminol in the presence of ferricyanide (detection limit was 0.45 µM) [ 85 ]. Later on, the pyridoxal 5’-phosphate containing enzyme D-serine dehydratase has been used for implementing a biosensor using fluorescein as dye-transducer to convert the change in cofactor absorption observed during the reaction on D-Ser into a change in fluorescence intensity [ 86 ]. More recently, a noninvasive system was constructed using luminescent DNA/silver nanoclusters (DNA/Ag NCs) to detect D-Ala and D-Pro as biomarkers to diagnose gastric cancer, merging D-AA oxidation and the Fenton reaction [ 76 ].…”