TAILIEUCHUNG - Báo cáo khoa học: D-Amino acids in the brain: the biochemistry of brain serine racemase

It has been recently established that in various brain regions d-serine, the product of serine racemase, occupies the so-called ‘glycine site’ within N-methyl d-aspartate receptors. Mammalian brain serine racemase is a pyridoxal-5¢ phosphate-containing enzyme that catalyzes the racemization ofl-serine to d-serine. | MINIREVIEW D-Amino acids in the brain the biochemistry of brain serine racemase Florian Baumgart and Ignacio Rodriguez-Crespo Departamento de Bioquimica y Biologia Molecular Facultad de Ciencias Quimicas Universidad Complutense de Madrid Spain Keywords AMPA receptor astrocytes ATP calcium activation D-serine gliotransmitters GRIP NMDA receptor PDZ interaction serine racemase Correspondence I. Rodriguez-Crespo Departamento de Bioquimica y Biologia Molecular Facultad de Ciencias Quimicas Universidad Complutense Ciudad Universitaria 28040 Madrid Spain Fax 34 91 394 4159 Tel 34 91394 4137 E-mail nacho@ Received 30 January 2008 revised 3 April 2008 accepted 4 April 2008 doi It has been recently established that in various brain regions D-serine the product of serine racemase occupies the so-called glycine site within N-methyl D-aspartate receptors. Mammalian brain serine racemase is a pyridoxal-5 phosphate-containing enzyme that catalyzes the racemization of L-serine to D-serine. It has also been shown to catalyze the a b-elimina-tion of water from L-serine or D-serine to form pyruvate and ammonia. Serine racemase is included within the group of type II-fold pyridoxal-5 phosphate enzymes together with many other racemases and dehydratases. Serine racemase was first purified from rat brain homogenates and later recombinantly expressed in mammalian and insect cells as well as in Escherichia coli. It has been shown that serine racemase is activated by divalent cations like calcium magnesium and manganese as well as by nucleotides like ATP ADP or GTP. In turn serine racemase is also strongly inhibited by reagents that react with free sulfhydryl groups such as glutathione. Several yeast two-hybrid screens for interaction partners identified the proteins glutamate receptor interacting protein protein interacting with C kinase 1 and Golga3 to bind to serine racemase having different effects on its catalytic activity or stability. In

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