Open Access
Review

Serine racemase: a key player in neuron activity and in neuropathologies

Barbara Campanini1,Francesca Spyrakis2,Alessio Peracchi3,Andrea Mozzarelli1,4,*
1
Department of Pharmacy, University of Parma, Parma, Italy
2
Department of Food Sciences, University of Parma, Parma, Italy
3
Department of Biosciences, University of Parma, Parma, Italy
4
National Institute of Biostructures and Biosystems, Rome, Italy
DOI: 10.2741/4167 Volume 18 Issue 3, pp.1112-1128
Published: 01 June 2013
(This article belongs to the Special Issue Biomedical aspects of pyridoxal phosphate dependent enzymes)
*Corresponding Author(s):  
Andrea Mozzarelli
E-mail:  
andrea.mozzarelli@unipr.it
Abstract

Serine racemase is the pyridoxal 5’-phosphatedependent enzyme that catalyzes L-serine racemisation to D-serine, and L- and D-serine beta-elimination in mammalian brain. D-serine is the essential co-agonist of the N-methyl-D-aspartate receptor, that mediates neurotransmission, synaptic plasticity, cell migration and long term potentiation. High and low D-serine levels have been associated with distinct neuropathologies, agingrelated deficits and psychiatric disorders due to either hyper- or hypo-activation of the receptor. Serine racemase dual activity is regulated by ATP, divalent cations, cysteine nitrosylation, post-translational modifications, and interactions with proteins that bind either at the N- or Cterminus. A detailed elucidation of the molecular basis of catalysis, regulation and conformational plasticity, as well as enzyme and D-serine localization and neurons and astrocytes cross-talk, opens the way to the development of enzyme inhibitors and effectors for tailored therapeutic treatments.

Key words

D-serine; NMDA receptor, Amino Acid Racemization, Catalysis, Pyridoxal 5’-Phosphate, Review

Share and Cite
Barbara Campanini, Francesca Spyrakis, Alessio Peracchi, Andrea Mozzarelli. Serine racemase: a key player in neuron activity and in neuropathologies. Frontiers in Bioscience-Landmark. 2013. 18(3); 1112-1128.