Mouse brain serine racemase catalyzes specific elimination of L-serine to pyruvate.

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Strisovsky K, Jiraskova J, Barinka C, Majer P, Rojas C, Slusher BS, Konvalinka J

Mouse brain serine racemase catalyzes specific elimination of L-serine to pyruvate.

FEBS Lett. 2003 Jan 30;535(1-3):44-8.

PubMed ID

12560076 [ View in PubMed

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Abstract

D-Serine was previously identified in mammalian brain and was shown to be a co-agonist at the 'glycine' site of the N-methyl-D-aspartate (NMDA)-type receptors. Racemization of serine is catalyzed by serine racemase, a pyridoxal 5'-phosphate-dependent enzyme expressed mainly in brain and liver. NMDA receptor overactivation has been implicated in a number of pathological conditions and inhibitors of serine racemase are thus potentially interesting targets for therapy. We expressed recombinant mouse serine racemase in insect cells and purified it to near homogeneity. The enzyme is a non-covalent homodimer in solution and requires divalent cations Mg(2+), Ca(2+) or Mn(2+) for activity but not for dimerization. In addition to the racemization it also catalyzes specific elimination of L-Ser to pyruvate. D-Serine is eliminated much less efficiently. Both L-serine racemization and elimination activities of serine racemase are of comparable magnitude, display alkaline pH optimum and are negligible below pH 6.5.

DrugBank Data that Cites this Article

Drug Targets

Drug	Target	Kind	Organism	Pharmacological Action	Actions
Pyridoxal phosphate	Serine racemase	Protein	Humans	Unknown	Cofactor	Details