Member database | CATH-Gene3D |
CATH-Gene3D type | homologous superfamily |
Description Imported from IPR042208
This superfamily represents a domain found in D-serine dehydratase, a zinc dependent enzyme involved in the degradation of D-serine, a physiological co-agonist of the NMDA receptor which is thus involved in the regulation of excitatory neurotransmission, important for higher brain functions in vertebrates. The primary structure of the enzyme shows significant similarities to that of metal-activated D-threonine aldolases, fold-type III pyridoxal 5'-phosphate (PLP)-dependent enzymes
[1, 2].
References Imported from IPR042208
1.Crystal structure of a zinc-dependent D-serine dehydratase from chicken kidney. Tanaka H, Senda M, Venugopalan N, Yamamoto A, Senda T, Ishida T, Horiike K. J. Biol. Chem. 286, 27548-58, (2011). View articlePMID: 21676877
2.Structural insights into the substrate stereospecificity of D-threo-3-hydroxyaspartate dehydratase from Delftia sp. HT23: a useful enzyme for the synthesis of optically pure L-threo- and D-erythro-3-hydroxyaspartate. Matsumoto Y, Yasutake Y, Takeda Y, Tamura T, Yokota A, Wada M. Appl. Microbiol. Biotechnol. 99, 7137-50, (2015). View articlePMID: 25715785