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Literature summary for 5.1.1.18 extracted from

  • Ohide, H.; Miyoshi, Y.; Maruyama, R.; Hamase, K.; Konno, R.
    D-Amino acid metabolism in mammals: biosynthesis, degradation and analytical aspects of the metabolic study (2011), J. Chromatogr. B, 879, 3162-3168.
    View publication on PubMed
Search for more literature for 5.1.1.18

Activating Compound

Activating Compound Comment Organism Structure
glutamate receptor interacting protein i.e. GRIP, the carboxy terminus of the mouse enzyme contains an amino acid domain that binds to PSD-95/DlgA/zo-1 (PDZ)-containing proteins, such as GRIP, which subsequently activates the racemase. The PDZ domain is an important protein-protein interaction motif Mus musculus
glutamate receptor interacting protein i.e. GRIP, the carboxy terminus of the mouse enzyme contains an amino acid domain that binds to PSD-95/DlgA/zo-1 (PDZ)-containing proteins, such as GRIP, which subsequently activates the racemase. The PDZ domain is an important protein-protein interaction motif Homo sapiens
additional information the enzyme is activated by nucleotides. Serine racemase can also be activated by phosphorylation Mus musculus
additional information the enzyme is activated by nucleotides. Serine racemase can also be activated by phosphorylation Homo sapiens
additional information the enzyme is activated by nucleotides. Serine racemase can also be activated by phosphorylation Rattus norvegicus
protein interacting with C kinase 1 i.e. PICK1, the carboxy terminus of the mouse enzyme contains an amino acid domain that binds to PSD-95/DlgA/zo-1 (PDZ)-containing proteins, such as PICK1, which subsequently activates the racemase. The PDZ domain is an important protein-protein interaction motif Mus musculus
protein interacting with C kinase 1 i.e. PICK1, the carboxy terminus of the mouse enzyme contains an amino acid domain that binds to PSD-95/DlgA/zo-1 (PDZ)-containing proteins, such as PICK1, which subsequently activates the racemase. The PDZ domain is an important protein-protein interaction motif Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
additional information S-nitrosylation or membrane binding inhibit racemase activity Homo sapiens
additional information S-nitrosylation or membrane binding inhibit racemase activity Mus musculus
additional information S-nitrosylation or membrane binding inhibit racemase activity Rattus norvegicus

Metals/Ions

Metals/Ions Comment Organism Structure
additional information the enzyme is activated by divalent cations Mus musculus
additional information the enzyme is activated by divalent cations Homo sapiens
additional information the enzyme is activated by divalent cations Rattus norvegicus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-serine Mus musculus
-
 D-serine
-
 ?
L-serine Homo sapiens
-
 D-serine
-
 ?
L-serine Rattus norvegicus
-
 D-serine
-
 ?
additional information Homo sapiens the enzyme binds to the glutamate receptor interacting protein, to protein interacting with C kinase 1, and Golgi-localized protein Golga 3 ?
-
 ?
additional information Mus musculus the enzyme binds to the glutamate receptor interacting protein, to protein interacting with C kinase 1, and Golgi-localized protein Golga 3. The carboxy terminus of both the mouse and human enzyme contains an amino acid domain that binds to PSD-95/DlgA/zo-1 (PDZ)-containing proteins, such as GRIP and PICK1, which subsequently activates the racemase. The PDZ domain is an important protein-protein interaction motif ?
-
 ?
additional information Rattus norvegicus the enzyme binds to the Golgi-localized protein Golga 3. The N-terminal of serine racemase contains residues that bind to Golga 3, which results in inhibition of ubiqitin-proteosomal serine racemase degradation ?
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-
Mus musculus
-
-
-
Rattus norvegicus
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
nitrosylation S-nitrosylation inhibits racemase activity Mus musculus
nitrosylation S-nitrosylation inhibits racemase activity Homo sapiens
nitrosylation S-nitrosylation inhibits racemase activity Rattus norvegicus
phosphoprotein serine racemase can be activated by phosphorylation Mus musculus
phosphoprotein serine racemase can be activated by phosphorylation Homo sapiens
phosphoprotein serine racemase can be activated by phosphorylation Rattus norvegicus

Source Tissue

Source Tissue Comment Organism Textmining
astrocyte protoplasmic Mus musculus
-
brain
-
 Mus musculus
-
cerebral cortex
-
 Mus musculus
-
corpus striatum
-
 Mus musculus
-
hippocampus
-
 Mus musculus
-
neuron the enzyme is present predominantly in the neurons Mus musculus
-
olfactory bulb
-
 Mus musculus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-serine
-
 Mus musculus D-serine
-
 ?
L-serine
-
 Homo sapiens D-serine
-
 ?
L-serine
-
 Rattus norvegicus D-serine
-
 ?
additional information the enzyme binds to the glutamate receptor interacting protein, to protein interacting with C kinase 1, and Golgi-localized protein Golga 3 Homo sapiens ?
-
 ?
additional information the enzyme binds to the glutamate receptor interacting protein, to protein interacting with C kinase 1, and Golgi-localized protein Golga 3. The carboxy terminus of both the mouse and human enzyme contains an amino acid domain that binds to PSD-95/DlgA/zo-1 (PDZ)-containing proteins, such as GRIP and PICK1, which subsequently activates the racemase. The PDZ domain is an important protein-protein interaction motif Mus musculus ?
-
 ?
additional information the enzyme binds to the Golgi-localized protein Golga 3. The N-terminal of serine racemase contains residues that bind to Golga 3, which results in inhibition of ubiqitin-proteosomal serine racemase degradation Rattus norvegicus ?
-
 ?

Subunits

Subunits Comment Organism
? x * 36000-37000 Mus musculus
? x * 36000-37000 Homo sapiens
? x * 36000-37000 Rattus norvegicus

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate dependent on, prosthetic group Mus musculus
pyridoxal 5'-phosphate dependent on, prosthetic group Homo sapiens
pyridoxal 5'-phosphate dependent on, prosthetic group Rattus norvegicus

General Information

General Information Comment Organism
malfunction mice genetically deficient in the serine racemase gene have decreased levels of D-serine in the brain. Serine racemase KO mice show no obvious defects, but neurotransmission and behavior mediated by the NMDA receptors are altered in these mice. The KO mice exhibit a schizophrenia-like phenotype and have impaired spatial memory, reduced prepulse inhibition, decreased sociability, and elevated anxiety. KO mice have a decreased level of D-serine, which protected against overstimulation of NMDA receptors Mus musculus
malfunction serine racemase is implicated with NMDA receptor dysfunction and schizophrenia Homo sapiens
additional information rat serine racemase lacks the C-terminal PDZrecognition sequence Rattus norvegicus
physiological function serine racemase activity is regulated by several physiological pathways. D-Serine binds to the coagonist site of the NMDA receptors and enhances neurotransmission Mus musculus
physiological function serine racemase activity is regulated by several physiological pathways. D-Serine binds to the coagonist site of the NMDA receptors and enhances neurotransmission Homo sapiens
physiological function serine racemase activity is regulated by several physiological pathways. D-Serine binds to the coagonist site of the NMDA receptors and enhances neurotransmission Rattus norvegicus