Mammalian serine racemase

Details Mammalian serine racemase Mammalian serine racemase

2006-01-10

2006-01-10

Slobodyansky, Elizabeth (Department: 1652)

Chemistry: molecular biology and microbiology

Measuring or testing process involving enzymes or...

C435S233000

Reexamination Certificate

active

06984484

ABSTRACT:
High levels of D-serine occur in mammalian brain, where it appears to be an endogenous ligand of the “glycine site” of NMDA receptors. We have purified from rat brain a soluble enzyme that catalyzes the direct racemization of L-serine to D-serine. Purified serine racemase has a molecular weight of 37 kDa and requires pyridoxal 5′-phosphate for its activity. The enzyme is highly selective toward L-serine, failing to racemize any other amino acid tested. We have also identified polynucleotide sequences that encode mammalian, including human, serine racemase. Compounds that modulate the activity of mammalian serine racemase are useful for treating conditions and diseases that involve overstimulation of NMDA receptors, such as stroke and various neurodegenerative diseases.

REFERENCES:
patent: 6458576 (2002-10-01), Meyers et al.
patent: 2048266 (1980-12-01), None
Takuma Uo et al, “Occurrence of pyridoxal 5'-phosphate-dependent Serine racemase in silkworm, Bombyx mori” Biochemical and Biophysical Research Communications, vol. 246, No. 1, May 8, 1998.
David S. Dunlop, et al., “The origin of turnover of D-Serine in brain” Biochemical and Biophysical Research Communications, vol. 235, No. 1, Jun. 9, 1997.
Herman Wolosker et al, “Serine racemase: a glial enzyme synthesizing D-Serine to regulate glutamate-N-methyl-D-asparate neurotransmission” Proceedings of the National Academy of Sciences of USA, vol. 96, No. 23, Nov. 9, 1999, pp. 13409-13414.
Hermann Wolosker, et al., Purification of Serine racemase: “Biosynthesis of the neuromodulator D-Serine”, Proceedings of the National Academy of Sciences of USA, vol. 96, No. 2, Jan. 19, 1999, pp. 721-725.

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