5.1.1.18: serine racemase
This is an abbreviated version!
For detailed information about serine racemase, go to the full flat file.
Word Map on EC 5.1.1.18
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5.1.1.18
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d-serine
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n-methyl-d-aspartate
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co-agonist
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nmdars
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astrocyte
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d-amino
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schizophrenia
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neurotransmission
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pyridoxal
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hypofunction
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d-aspartate
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glutamatergic
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5'-phosphate-dependent
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nmda-type
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d-ser
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plp-dependent
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nmdar-mediated
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pharmacology
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medicine
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alanine-serine-cysteine
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drug development
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glycine-binding
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n-methyl-d
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vante
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brain-enriched
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gliotransmitter
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nmdar-dependent
- 5.1.1.18
- d-serine
- n-methyl-d-aspartate
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co-agonist
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nmdars
- astrocyte
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d-amino
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schizophrenia
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neurotransmission
- pyridoxal
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hypofunction
- d-aspartate
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glutamatergic
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5'-phosphate-dependent
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nmda-type
- d-ser
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plp-dependent
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nmdar-mediated
- pharmacology
- medicine
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alanine-serine-cysteine
- drug development
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glycine-binding
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n-methyl-d
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vante
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brain-enriched
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gliotransmitter
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nmdar-dependent
Reaction
Synonyms
hSR, More, RiSR, RLO149_c015450, Ser racemase, SerR, SRace, SRR, T01H8.2, Zm-SR, ZmSR
ECTree
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Activating Compound
Activating Compound on EC 5.1.1.18 - serine racemase
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1,4-dithiothreitol
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chemical reduction with DTT increases the enzyme activity by elevating Vmax
hydroxylamine
activates Ser racemase activity, but inhibits Asp racemase activity
metabotropic glutamate receptor
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i.e. mGluR5, on glia, activation mechanism of the D-serine synthesis needed for NMDA neurotransmission, overview
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morphine
chronic administration significantly augments both serine racemase mRNA and protein expression in all brain regions and leads to slight but significant elevation in the concentration of D-serine in the cortex, striatum, and hippocampus
ATP
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ATP binding to human serine racemase is strongly cooperative and modulated by glycine, the active-site ligand increases the serine racemase affinity for ATP by about 22fold, abolishing cooperativity. ATP increases the noncooperative glycine binding15fold
ATP
activates the enzyme independently from Mg2+, the nucleotide increases serine racemase activity even in the presence of EDTA, and the effect due to divalent ion and ATP is additive. In the presence of 1 mM ATP, the Km for L-serine is decreased 10fold with little change in Vmax
ATP
the enzyme is allosterically controlled by ATP, which increases its activity around 7fold through a cooperative binding mechanism
ATP
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1 mM, decrease of Km-value for racemization by 85%, allosteric mechanism. Inhibitory to L-serine O-sulfate dehydration reaction
ATP
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competes with inhibitor phosphatidylinositol(4,5)-bisphosphate for enzyme binding
ATP
activates the enzyme independently from Mg2+, the nucleotide increases serine racemase activity even in the presence of EDTA, and the effect due to divalent ion and ATP is additive. In the presence of 1 mM ATP, the Km for L-serine is decreased 10fold with little change in Vmax
ATP
MgATP- enhances both activities of RiSR, racemization and dehydration. At 1 mM MgATP on dehydration and racemization activities are enhanced 3fold and 13fold, respectively
ATP
as MgATP2-, the ATP binding site is located at the domain and the subunit interface
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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
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glutamate receptor interacting protein
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i.e. GRIP, a multi-PSD-95/discs large/ZO-1 domain protein, that is usually coupled to the GluR2/3 subunits of the alpha-amino-3-hydroxy-5-methylisoxazole-4-propionic acid Ca2+ channel, in vivo activation by full-length GRIP, determination of required length and domains of the protein for activation, activation mechanism, overview
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glutamate receptor interacting protein
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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
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glycine stabilizes a protein conformation that binds ATP non-cooperatively and with high affinity, the active-site ligand increases the serine racemase affinity for ATP by about 22fold, abolishing cooperativity. ATP increases the noncooperative glycine binding 15fold
glycine
active site ligand glycine increases the enzyme's affinity for ATP by 22fold and abolishes cooperativity while ATP increases the noncooperative glycine binding 15fold
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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
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protein interacting with C kinase 1
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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
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EDTA has no significant effect on enzyme activity
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additional information
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EDTA has no significant effect on enzyme activity
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additional information
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the enzyme is activated by nucleotides. Serine racemase can also be activated by phosphorylation
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additional information
EDTA has no significant effect on enzyme activity
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additional information
the enzyme requires pyridoxal 5'-phosphate and divalent cations such as Ca2+, Mg2+, or Mn2+, but not ATP
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additional information
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the enzyme requires pyridoxal 5'-phosphate and divalent cations such as Ca2+, Mg2+, or Mn2+, but not ATP
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additional information
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activation of enzyme by glutamate neurotransmission involving alpha-amino-3-hydroxy-5-methylisoxazole-4-propionic acid receptors
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additional information
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activation of serine racemase by divalent cations has been assumed to be a side-effect associated with ATP binding, activation mechanisms and ligand binding, molecular modelling with the human enzyme, overview
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additional information
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the glutamate transmission activates the enzyme by degrading phospholipids
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additional information
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the enzyme is activated by nucleotides. Serine racemase can also be activated by phosphorylation
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additional information
no effect on Ser racemase activity by EDTA, KCl, and NaCl. Asp racemization is activated by divalent cations and nucleotide complexes
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additional information
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ketamine, a noncompetitive N-methyl-D-aspartate receptor antagonist, ketamine, transiently enhances the expression of the enzyme in the brain in all the brain areas, overview
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additional information
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non-competitive N-methyl-D-aspartate receptor antagonist MK-801 causes an increase of serine racemase and D-serine levels in almost all brain areas, e.g. in striatum, hippocampus, cortex, diencephalon, midbrain, pons-medulla, and cerebellum, overview
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additional information
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the amyloid beta-peptide and secreted forms, liberated by alpha- or beta-secretase, of beta-amyloid precursor protein induce enzyme expression and lead to elevated D-serine levels in microglia, overview
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additional information
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the enzyme is activated by nucleotides. Serine racemase can also be activated by phosphorylation
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