PXLP-K56-SRR dimer deaminates D-Ser

Stable Identifier
R-HSA-9014741
Type
Reaction [transition]
Species
Homo sapiens
Compartment
Locations in the PathwayBrowser
General
SVG |   | PPTX  | SBGN
Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout

N-methyl D-aspartate (NMDA) receptors play a key role in excitatory neurotransmission, learning, memory and synaptic plasticity. Their activity is modulated by the agonist glutamate and by the co-agonists D-Serine (D-Ser) and glycine (gly). In human brain, dimeric serine racemase (SRR), a pyridoxal 5'-phosphate-dependent enzyme (Smith et al. 2010), is a bifunctional enzyme mediating deamination and isomerisation of L-Serine. It can also catabolise D-Serine by alpha,beta-elimination of water to form pyruvate but at a rate 10-fold lower than for L-Serine (De Miranda et al. 2000, 2002, Foltyn et al. 2005). Thus, D-Ser homeostasis in neurons is modulated by SRR, and therefore indirectly, modulates NMDA receptors. Targeting SRR could find potential in neurodegenerative diseases (Canu et al. 2014). Mg2+ and ATP stimulate SRR (De Miranda et al. 2002).

Literature References
PubMed ID Title Journal Year
12393813 Cofactors of serine racemase that physiologically stimulate the synthesis of the N-methyl-D-aspartate (NMDA) receptor coagonist D-serine

De Miranda, J, Panizzutti, R, Foltyn, VN, Wolosker, H

Proc. Natl. Acad. Sci. U.S.A. 2002
15536068 Serine racemase modulates intracellular D-serine levels through an alpha,beta-elimination activity

Foltyn, VN, Bendikov, I, De Miranda, J, Panizzutti, R, Dumin, E, Shleper, M, Li, P, Toney, MD, Kartvelishvily, E, Wolosker, H

J. Biol. Chem. 2005
Participants
Participant Of
Catalyst Activity
Catalyst Activity
Title
D-serine ammonia-lyase activity of PXLP-K56-SRR dimer [cytosol]
Physical Entity
Activity
This event is regulated
Orthologous Events
Cross References
Rhea
Authored
Reviewed
Created