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

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

Document Type: Research Article


Affiliations: Laboratory for Molecular Sensing, IBP-CNR Via Pietro Castellino, 111 801131 Naples, Italy.

Publication date: June 1, 2012

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.

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