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.
Keywords: Fluorescence, biosensors, D-Serine dehydratase, absorption, pyridoxal 5'-phosphate, fluorescence spectroscopy, NMDA (N-methyl-D-aspartate), D-serine, neuro-diseases, enzymatic assays
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