Abstract

D-Aspartate (D-Asp) is found in specific neurons, transported to neuronal terminals and released in a stimulation-dependent manner. Because D-Asp formation is not well understood, determining its function has proved challenging. Significant levels of D-Asp are present in the cerebral ganglion of the F- and C-clusters of the invertebrate Aplysia californica, and D-Asp appears to be involved in cell-cell communication in this system. Here, we describe a novel protein, DAR1, from A. californica that can convert aspartate and serine to their other chiral form in a pyridoxal 5'-phosphate (PLP)-dependent manner. DAR1 has a predicted length of 325 amino acids and is 55% identical to the bivalve aspartate racemase, EC 5.1.1.13, and 41% identical to the mammalian serine racemase, EC 5.1.1.18. However, it is only 14% identical to the recently reported mammalian aspartate racemase, DR, which is closely related to glutamate-oxaloacetate transaminase, EC 2.6.1.1. Using whole-mount immunohistochemistry staining of the A. californica central nervous system, we localized DAR1-like immunoreactivity to the medial region of the cerebral ganglion where the F- and C-clusters are situated. The biochemical and functional similarities between DAR1 and other animal serine and aspartate racemases make it valuable for examining PLP-dependent racemases, promising to increase our knowledge of enzyme regulation and ultimately, D-serine and D-Asp signaling pathways.

Original languageEnglish (US)
Pages (from-to)13765-13774
Number of pages10
JournalJournal of Biological Chemistry
Volume286
Issue number15
DOIs
StatePublished - Apr 15 2011

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aspartate racemase
Amino Acid Isomerases
D-Aspartic Acid
Aplysia
Pyridoxal Phosphate
Neurology
Central Nervous System
Ganglia
Serine
Racemases and Epimerases
Oxaloacetic Acid
Bivalvia
Invertebrates
Aspartate Aminotransferases
Transaminases
Aspartic Acid
Cell Communication
Neurons
Glutamic Acid
Animals

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

A novel pyridoxal 5'-phosphate-dependent amino acid racemase in the aplysia californica central nervous system. / Wang, Liping; Ota, Nobutoshi; Romanova, Elena V.; Sweedler, Jonathan V.

In: Journal of Biological Chemistry, Vol. 286, No. 15, 15.04.2011, p. 13765-13774.

Research output: Contribution to journalArticle

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