SRR
SRR (serine racemase) is a pyridoxal-5'-phosphate-dependent enzyme that catalyses the synthesis of D-serine from L-serine. D-serine acts as a key coagonist with glutamate at NMDA receptors; the gene is also known as ILV1 and ISO1. Browse Assay Genie's current range of SRR research reagents below, or read on for the biology behind the target.
SRR is a pyridoxal-5'-phosphate (PLP)-dependent enzyme that catalyses the conversion of L-serine to D-serine. D-serine is a key coagonist with glutamate at NMDA receptors, which places this enzyme at the centre of work on glutamatergic signalling. In addition to racemisation, SRR has dehydratase activity towards both L-serine and D-serine. This is a two-step reaction: the hydroxyl group of serine is first eliminated to give aminoacrylate (2-aminoprop-2-enoate), and this unstable intermediate is then deaminated by nonenzymatic hydrolysis to produce pyruvate.
The SRR gene encodes serine racemase, which belongs to the serine/threonine dehydratase family. HGNC places it in the carbon-nitrogen lyases gene group, and the enzyme carries the EC number 5.1.1.18. Mouse and rat both have an orthologous Srr gene, so the protein can be studied in common rodent models. Studies of the SRR protein typically focus on its role in D-serine production and on its competing L-serine ammonia-lyase activity.
According to the NCBI Gene summary, SRR enables L-serine ammonia-lyase activity, PDZ domain binding and heterocyclic compound binding. It is involved in oxoacid metabolic processes and in the response to lipopolysaccharide, and it is located in the cytoplasm and in the neuronal cell body. The aliases ILV1 and ISO1 are used in some databases and publications for the same gene.
SRR makes D-serine, a key coagonist with glutamate at NMDA receptors, so it is a focus for studies of glutamatergic neurotransmission.
SRR is located in the cytoplasm and neuronal cell body, making it relevant to studies of where D-serine synthesis occurs in neurons.
SRR combines racemase and dehydratase activities, producing aminoacrylate and then pyruvate, which offers a model for PLP-dependent catalysis.
The gene is annotated as involved in the response to lipopolysaccharide, linking SRR to studies of cellular responses to bacterial stimuli.
SRR is a PLP-dependent enzyme that synthesises D-serine from L-serine. D-serine is a key coagonist with glutamate at NMDA receptors. SRR also has dehydratase activity on both serine forms, producing aminoacrylate that is then hydrolysed nonenzymatically to pyruvate.
The HGNC-approved name is serine racemase, and UniProt uses the same protein name. Aliases include ILV1 and ISO1. The enzyme is classified as EC 5.1.1.18 and belongs to the serine/threonine dehydratase family within the carbon-nitrogen lyases gene group.
Yes. Both mouse and rat have an orthologous gene named Srr, which allows the enzyme to be studied in rodent models. Cross-reactivity differs between reagents, so check the datasheet of any product for its validated reactivity.
Other NMDA receptor components, D-amino acid metabolism enzymes and serine pathway proteins with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt Q9GZT4; product specifications from Assay Genie datasheets.