serine racemase activity

Definition

Target type: molecularfunction

Catalysis of the synthesis of free D-serine from L-serine. [GOC:kd]

Serine racemase activity is a crucial enzymatic function that interconverts L-serine and D-serine, stereoisomers of the amino acid serine. This interconversion is essential for various physiological processes, particularly in the nervous system. D-serine acts as a co-agonist for the NMDA receptor, a glutamate receptor involved in synaptic plasticity and memory formation. Serine racemase, the enzyme responsible for this interconversion, catalyzes the epimerization of L-serine to D-serine through a pyridoxal-5'-phosphate (PLP)-dependent mechanism. The enzyme utilizes PLP as a cofactor, which forms a Schiff base with the amino group of serine. This Schiff base undergoes a series of rearrangements and protonation events, leading to the inversion of the stereochemistry at the alpha carbon of serine. The precise molecular mechanism involves the formation of a quinonoid intermediate, followed by protonation from the opposite side of the molecule, resulting in the production of D-serine. The activity of serine racemase is tightly regulated, ensuring the appropriate levels of D-serine for optimal neuronal function. Dysregulation of serine racemase activity has been linked to various neurological disorders, including schizophrenia and Alzheimer's disease, highlighting its importance in maintaining brain health.'
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Proteins (1)

Compounds (9)