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Information on EC 5.1.1.18 - serine racemase and Organism(s) Mus musculus and UniProt Accession Q9QZX7

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     5 Isomerases
         5.1 Racemases and epimerases
             5.1.1 Acting on amino acids and derivatives
                5.1.1.18 serine racemase
IUBMB Comments
A pyridoxal-phosphate protein that is highly selective for L-serine as substrate. D-Serine is found in type-II astrocytes in mammalian brain, where it appears to be an endogenous ligand of the glycine site of N-methyl-D-aspartate (NMDA) receptors [1,2]. The reaction can also occur in the reverse direction but does so more slowly at physiological serine concentrations .
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This record set is specific for:
Mus musculus
UNIPROT: Q9QZX7
Word Map
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The taxonomic range for the selected organisms is: Mus musculus
Reaction Schemes
Synonyms
hSR, More, RiSR, RLO149_c015450, Ser racemase, SerR, SRace, SRR, T01H8.2, Zm-SR, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SerR
278079
-
additional information
278079
cf. EC 5.1.1.13
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-serine = D-serine
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
elimination
-
-
racemization
-
-
SYSTEMATIC NAME
IUBMB Comments
serine racemase
A pyridoxal-phosphate protein that is highly selective for L-serine as substrate. D-Serine is found in type-II astrocytes in mammalian brain, where it appears to be an endogenous ligand of the glycine site of N-methyl-D-aspartate (NMDA) receptors [1,2]. The reaction can also occur in the reverse direction but does so more slowly at physiological serine concentrations [4].
CAS REGISTRY NUMBER
COMMENTARY hide
77114-08-0
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-aspartate
D-aspartate
show the reaction diagram
L-serine
D-serine
show the reaction diagram
beta-chloro-L-alanine
pyruvate + NH3 + ?
show the reaction diagram
-
the artificial serine racemase substrate is degraded via alpha,beta-elimination
-
-
?
D-serine
L-serine
show the reaction diagram
D-serine
pyruvate + H2O
show the reaction diagram
-
alpha,beta-elimination reaction
-
-
?
D-serine
pyruvate + NH3
show the reaction diagram
D-serine
S-serine
show the reaction diagram
-
-
-
-
?
L-serine
D-serine
show the reaction diagram
L-serine
pyruvate + NH3
show the reaction diagram
L-serine O-sulfate
O-sulfopyruvate + NH3
show the reaction diagram
L-serine O-sulfate
pyruvate + NH3 + ?
show the reaction diagram
-
the artificial serine racemase substrate is degraded via alpha,beta-elimination
-
-
?
L-threo-3-hydroxyaspartate
pyruvate + NH3 + ?
show the reaction diagram
-
the artificial serine racemase substrate is degraded via alpha,beta-elimination
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
-
alpha,beta-elimination reaction
-
-
?
L-threonine
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-aspartate
D-aspartate
show the reaction diagram
-
-
-
-
r
L-serine
D-serine
show the reaction diagram
L-serine
D-serine
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
-
ATP
-
Mg-ATP is a stimulatory cofactor
pyridoxal 5'-phosphate
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
activates
EDTA
-
complete inhibition, provokes a profound conformational change
additional information
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
amino-oxyacetic acid
-
complete inhibition
beta-haloalanine
-
reacts with pyridoxal 5'-phosphate to yield thiazolidine derivative
cysteine
-
reacts with pyridoxal 5'-phosphate to yield thiazolidine derivative
glycine
-
competitive
homocysteine
-
reacts with pyridoxal 5'-phosphate to yield thiazolidine derivative
L-aspartate
-
competitive
nitric oxide
-
nitric oxide physiologically S-nitrosylates the enzyme at Cys113, mediating feedback inhibition of D-serine, which is enhanced by the NMDA receptor through activation of neuronal nitric oxide synthase
Acetohydroxamic acid
-
i.e. Lithostat
adipodihydroxamic acid
-
-
aminooxyacetic acid
-
non-selective inhibitor
beta-chloro-L-alanine
-
2 mM, 68% residual activity
beta-fluoro-D,L-alanine
-
2 mM, 81% residual activity
Co2+
-
-
Cu2+
-
-
cystamine
-
50% inhibition at 0.0081 mM
D-cysteine
-
2 mM, 72% residual activity
Dihydroxyfumarate
-
-
DL-Serine hydroxamate
-
-
DL-Threonine hydroxamate
-
-
Fe2+
-
slight inhibition of both activities
glutarodihydroxamic acid
-
-
glycine
Glycine hydroxamate
-
-
L-2,3-diaminopropionic acid
-
2 mM, 68% residual activity
L-asparagine
L-aspartic acid
L-aspartic acid beta-hydroxamate
-
a competitive and selective serine racemase inhibitor
L-Cycloserine
-
10 mM, 45% inhibition
L-cysteine
L-cysteine-S-sulfate
-
-
L-erythro-3-hydroxyaspartate
L-homocysteic acid
-
2 mM, 59% residual activity
L-serine-O-sulfate
Maleate
-
-
malonate
malonodihydroxamic acid
-
-
meso-tartrate
-
-
Ni2+
-
slight inhibition of both activities
oxaloacetic acid
-
2 mM, 56% residual activity
oxalodihydroxamic acid
-
-
phenazine
-
non-selective inhibitor
phosphatidylinositol-4,5-bisphosphate
-
i.e. PIP2, a physiological inhibitor of the enzyme, competes with activator ATP for enzyme binding. Activation of metabotropic glutamate receptors on glia leads to phospholipase C-mediated degradation of PIP2, relieving SR inhibition
suberodihydroxamic acid
-
-
succinodihydroxamic acid
-
-
vorinostat
-
i.e. Zolinza
Zn2+
-
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
hydroxylamine
-
activates Ser racemase activity, but inhibits Asp racemase activity
glutamate receptor interacting protein
-
metabotropic glutamate receptor
-
i.e. mGluR5, on glia, activation mechanism of the D-serine synthesis needed for NMDA neurotransmission, overview
-
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
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
20.9 - 172
D-serine
3.8 - 69.9
L-serine
3.2 - 75
D-serine
1.8 - 75
L-serine
0.49
L-serine O-sulfate
-
pH 8.0, 37C, presence of 1 mM ATP, elimination reaction
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.285 - 5.68
D-serine
0.277 - 5.71
L-serine
0.004 - 14.5
D-serine
0.02 - 4
L-serine
0.49
L-serine O-sulfate
-
pH 8.0, 37C, presence of 1 mM ATP, elimination reaction
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00477 - 0.195
D-serine
0.00518 - 0.202
L-serine
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.69
Dihydroxyfumarate
-
pH 8.0, 37C
1.64
glycine
1.13
L-asparagine
-
pH 8.0, 37C
1.9
L-aspartic acid
1.3
L-aspartic acid beta-hydroxamate
-
pH 8.0
0.64
L-cysteine-S-sulfate
-
pH 8.0, 37C
0.043
L-erythro-3-hydroxyaspartate
0.55
Maleate
-
pH 8.0, 37C
0.071
malonate
0.66
meso-tartrate
-
pH 8.0, 37C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.013
phosphatidylinositol-4,5-bisphosphate
Mus musculus
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
16.2
-
pH 8.0
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.7
-
assay at
8
-
assay at
8 - 9.5
-
-
8
-
assay at
8.1
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5
-
negligible activity below
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
assay at
37
-
assay at
37
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
increase of enzyme expression after birth
Manually annotated by BRENDA team
-
of adult cerebellum, weak but significant expression
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
high expression level, especially in neocortex and hippocampus
Manually annotated by BRENDA team
-
primary ganglion cell, robust expression of serine racemase
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
epidermal
Manually annotated by BRENDA team
-
developmental regulation of enzyme expression, in situ hybridization analysis, overview, D-serine levels are quite high in ganglion cells of neonatal retinas and decreasing rapidly postnatally
Manually annotated by BRENDA team
-
localization of the enzme protein in the granular and cornified layer of the epidermis
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
-
SerRs and AspRs are not separated by their racemase functions and form a serine/aspartate racemase family cluster based on phylogenetic analysis
malfunction
physiological function
malfunction
physiological function
additional information
-
role of individual residues at position 150-152, overview
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
SRR_MOUSE
339
0
36359
Swiss-Prot
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
36300
-
x * 36300, calculated, x * 38000, SDS-PAGE
38000
-
x * 36300, calculated, x * 38000, SDS-PAGE
29000
-
x * 29000, truncated mutant enzyme, SDS-PAGE
36121
-
x * 36121, MALDI-MS, x * 36123, calculated
36123
-
x * 36121, MALDI-MS, x * 36123, calculated
37000
37500
-
2 * 37500, SDS-PAGE, dimer-tetramer equilibrium; 4 * 37500, SDS-PAGE, dimer-tetramer equilibrium
38000
-
x * 38000, SDS-PAGE
55000
-
isoforms A and B, gel filtration
78000
-
gel filtration
82900
-
gel filtration
153000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 36300, calculated, x * 38000, SDS-PAGE
homodimer
-
dimeric structure, overview
dimer
tetramer
-
4 * 37500, SDS-PAGE, dimer-tetramer equilibrium
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nitrosylation
-
S-nitrosylation inhibits racemase activity
phosphoprotein
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C113S
-
site-directed mutagenesis, the mutant is resistant to regulation by nitrosylation by NO
H150S
-
site-directed mutagenesis, the mutant shows altered substrate specificity and activity compared to the wild-type enzyme
H150S/N152S
-
site-directed mutagenesis, the mutant shows altered substrate specificity and activity compared to the wild-type enzyme
H150S/P151S
-
site-directed mutagenesis, the mutant shows altered substrate specificity and activity compared to the wild-type enzyme
H150S/P151S/N152S
-
site-directed mutagenesis, the mutant shows altered substrate specificity and activity compared to the wild-type enzyme
K51A
-
site-directed mutagenesis, the K51A mutant shows substantially less ATP binding and reduced activity compared to the wild-type enzyme
N152S
-
site-directed mutagenesis, the mutant shows altered substrate specificity and activity compared to the wild-type enzyme
P151S
-
site-directed mutagenesis, the mutant shows altered substrate specificity and activity compared to the wild-type enzyme
P151S/N152S
-
site-directed mutagenesis, the mutant shows altered substrate specificity and activity compared to the wild-type enzyme
Q155D
-
site-directed mutagenesis, catalytically hyperactive mutant, the mutant shows enhanced racemization and reduced alpha,beta-elimination activities
S84A
-
site-directed mutagenesis, SRR mutant S84A shows Ser dehydratase activity, but no Ser racemase activity, the S84A mutation completely abolishes racemization activity for both Ser and Asp. Mutation S84A results in the loss of the enzyme's D-Ser dehydrase activity without changing L-Ser dehydrase activity
H152S
-
ratio of elimination reaction to racemization is 1.4 compared to 3.7 in wild-type
K56G
-
inactive
N154F
-
ratio of elimination reaction to racemization is 0.33 compared to 3.7 in wild-type
P153S
-
ratio of elimination reaction to racemization is 0.24 compared to 3.7 in wild-type
Q155D
-
ratio of elimination reaction to racemization is 0.25 compared to 3.7 in wild-type
additional information
PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and dialysis
-
recombinant His6-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) using Talon resin chromatography
-
both isoforms A and B
-
recombinant enzyme expressed in insect cells
-
recombinant enzyme from Escherichia coli strain MC1061 by hydrophobic interaction and anion exchange chromatography, followed by ATP affinity chromatography and dialysis
-
CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
expression of His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
-
gene Srr, recombinant expression of wild-type and mutant enzymes in Rattus norvegicus PC-12 cells, recombinant expression of N-terminally His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3). SRR-overexpressing PC-12 cells produce endogenous D-Asp and D-Ser
-
gene SRR, sequence comparisons and phylogenetic tree
-
recombinant expression of His-tagged wild-type and mutant enzymes in HEK-293T cells
-
enzyme expression in Escherichia coli strain MC1061
-
expression of GST-tagged fusion protein containing amino acid residue 150-190 of the mouse enzyme, expression of His-tagged enzyme in Cavia porcellus and Oryctolagus cuniculus, quantitative real-time PCR enzyme expression analysis
-
expression of untagged and of N-terminally His6-tagged and C-terminally FLAG-tagged enzyme in COS-7 cells, co-expression with glutamate receptor interacting protein or FLAG-tagged glutamate receptor interacting protein domain PDZ6
-
HEK293 cells transfected with wild-type enzyme and metabotropic glutamate receptor display a 4fold increase in enzyme activity upon treatment with the metabotropic glutamate receptor agonist dihydroxyphenylglycine
-
quantitative expression analysis
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wang, L.Z.; Zhu, X.Z.
Spatiotemporal relationships among D-serine, serine racemase, and D-amino acid oxidase during mouse postnatal development
Acta Pharmacol. Sin.
24
965-974
2003
Mus musculus
Manually annotated by BRENDA team
Strisovsky, K.; Jiraskova, J.; Mikulova, A.; Rulisek, L.; Konvalinka, J.
Dual substrate and reaction specificity in mouse serine racemase: identification of high-affinity dicarboxylate substrate and inhibitors and analysis of the beta-eliminase activity
Biochemistry
44
13091-13100
2005
Mus musculus, Mus musculus (Q9QZX7)
Manually annotated by BRENDA team
Dunlop, D.S.; Neidle, A.
Regulation of serine racemase activity by amino acids
Brain Res. Mol. Brain Res.
133
208-214
2005
Mus musculus
Manually annotated by BRENDA team
Strisovsky, K.; Jiraskova, J.; Barinka, C.; Majer, P.; Rojas, C.; Slusher, B.S.; Konvalinka, J.
Mouse brain serine racemase catalyzes specific elimination of L-serine to pyruvate
FEBS Lett.
535
44-48
2003
Mus musculus, Mus musculus (Q9QZX7)
Manually annotated by BRENDA team
Cook, S.P.; Galve-Roperh, I.; Martinez del Pozo, A.; Rodriguez-Crespo, I.
Direct calcium binding results in activation of brain serine racemase
J. Biol. Chem.
277
27782-27792
2002
Mus musculus
Manually annotated by BRENDA team
Foltyn, V.N.; Bendikov, I.; De Miranda, J.; Panizzutti, R.; Dumin, E.; Shleper, M.; Li, P.; Toney, M.D.; Kartvelishvily, E.; Wolosker, H.
Serine racemase modulates intracellular D-serine levels through an alpha,beta-elimination activity
J. Biol. Chem.
280
1754-1763
2005
Mus musculus
Manually annotated by BRENDA team
Neidle, A.; Dunlop, D.S.
Allosteric regulation of mouse brain serine racemase
Neurochem. Res.
27
1719-1724
2002
Mus musculus
Manually annotated by BRENDA team
Stevens, E.R.; Esguerra, M.; Kim, P.M.; Newman, E.A.; Snyder, S.H.; Zahs, K.R.; Miller, R.F.
D-serine and serine racemase are present in the vertebrate retina and contribute to the physiological activation of NMDA receptors
Proc. Natl. Acad. Sci. USA
100
6789-6794
2003
Ambystoma tigrinum, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Kim, P.M.; Aizawa, H.; Kim, P.S.; Huang, A.S.; Wickramasinghe, S.R.; Kashani, A.H.; Barrow, R.K.; Huganir, R.L.; Ghosh, A.; Snyder, S.H.
Serine racemase: activation by glutamate neurotransmission via glutamate receptor interacting protein and mediation of neuronal migration
Proc. Natl. Acad. Sci. USA
102
2105-2110
2005
Mus musculus
Manually annotated by BRENDA team
Wolosker, H.; Blackshaw, S.; Snyder, S.H.
Serine racemase: a glial enzyme synthesizing D-serine to regulate glutamate-N-methyl-D-aspartate neurotransmission
Proc. Natl. Acad. Sci. USA
96
13409-13414
1999
Mus musculus (Q9QZX7)
Manually annotated by BRENDA team
De Miranda, J.; Panizzutti, R.; Foltyn, V.N.; Wolosker, H.
Cofactors of serine racemase that physiologically stimulate the synthesis of the N-methyl-D-aspartate (NMDA) receptor coagonist D-serine
Proc. Natl. Acad. Sci. USA
99
14542-14547
2002
Mus musculus
Manually annotated by BRENDA team
Baumgart, F.; Mancheno, J.M.; Rodriguez-Crespo, I.
Insights into the activation of brain serine racemase by the multi-PDZ domain glutamate receptor interacting protein, divalent cations and ATP
FEBS J.
274
4561-4571
2007
Mus musculus
Manually annotated by BRENDA team
Dun, Y.; Duplantier, J.; Roon, P.; Martin, P.M.; Ganapathy, V.; Smith, S.B.
Serine racemase expression and D-serine content are developmentally regulated in neuronal ganglion cells of the retina
J. Neurochem.
104
970-978
2007
Mus musculus, Mus musculus C57/BL6J
Manually annotated by BRENDA team
Mustafa, A.K.; Kumar, M.; Selvakumar, B.; Ho, G.P.; Ehmsen, J.T.; Barrow, R.K.; Amzel, L.M.; Snyder, S.H.
Nitric oxide S-nitrosylates serine racemase, mediating feedback inhibition of D-serine formation
Proc. Natl. Acad. Sci. USA
104
2950-2955
2007
Mus musculus (Q9QZX7)
Manually annotated by BRENDA team
Hikida, T.; Mustafa, A.K.; Maeda, K.; Fujii, K.; Barrow, R.K.; Saleh, M.; Huganir, R.L.; Snyder, S.H.; Hashimoto, K.; Sawa, A.
Modulation of D-serine levels in brains of mice lacking PICK1
Biol. Psychiatry
63
997-1000
2008
Mus musculus
Manually annotated by BRENDA team
Miya, K.; Inoue, R.; Takata, Y.; Abe, M.; Natsume, R.; Sakimura, K.; Hongou, K.; Miyawaki, T.; Mori, H.
Serine racemase is predominantly localized in neurons in mouse brain
J. Comp. Neurol.
510
641-654
2008
Mus musculus
Manually annotated by BRENDA team
Inoue, R.; Hashimoto, K.; Harai, T.; Mori, H.
NMDA- and beta-amyloid1-42-induced neurotoxicity is attenuated in serine racemase knock-out mice
J. Neurosci.
28
14486-14491
2008
Mus musculus
Manually annotated by BRENDA team
Basu, A.C.; Tsai, G.E.; Ma, C.L.; Ehmsen, J.T.; Mustafa, A.K.; Han, L.; Jiang, Z.I.; Benneyworth, M.A.; Froimowitz, M.P.; Lange, N.; Snyder, S.H.; Bergeron, R.; Coyle, J.T.
Targeted disruption of serine racemase affects glutamatergic neurotransmission and behavior
Mol. Psychiatry
14
719-727
2008
Mus musculus
Manually annotated by BRENDA team
Hoffman, H.E.; Jiraskova, J.; Ingr, M.; Zvelebil, M.; Konvalinka, J.
Recombinant human serine racemase: enzymologic characterization and comparison with its mouse ortholog
Protein Expr. Purif.
63
62-67
2009
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Labrie, V.; Fukumura, R.; Rastogi, A.; Fick, L.J.; Wang, W.; Boutros, P.C.; Kennedy, J.L.; Semeralul, M.O.; Lee, F.H.; Baker, G.B.; Belsham, D.D.; Barger, S.W.; Gondo, Y.; Wong, A.H.; Roder, J.C.
Serine racemase is associated with schizophrenia susceptibility in humans and in a mouse model
Hum. Mol. Genet.
18
3227-3243
2009
Homo sapiens, Mus musculus, Mus musculus C57BL/6JJcl
Manually annotated by BRENDA team
Hoffman, H.E.; Jiraskova, J.; Cigler, P.; Sanda, M.; Schraml, J.; Konvalinka, J.
Hydroxamic acids as a novel family of serine racemase inhibitors: mechanistic analysis reveals different modes of interaction with the pyridoxal-5'-phosphate cofactor
J. Med. Chem.
52
6032-6041
2009
Mus musculus
Manually annotated by BRENDA team
Mustafa, A.K.; Ahmad, A.S.; Zeynalov, E.; Gazi, S.K.; Sikka, G.; Ehmsen, J.T.; Barrow, R.K.; Coyle, J.T.; Snyder, S.H.; Dore, S.
Serine racemase deletion protects against cerebral ischemia and excitotoxicity
J. Neurosci.
30
1413-1416
2010
Mus musculus
Manually annotated by BRENDA team
Mustafa, A.K.; van Rossum, D.B.; Patterson, R.L.; Maag, D.; Ehmsen, J.T.; Gazi, S.K.; Chakraborty, A.; Barrow, R.K.; Amzel, L.M.; Snyder, S.H.
Glutamatergic regulation of serine racemase via reversal of PIP2 inhibition
Proc. Natl. Acad. Sci. USA
106
2921-2926
2009
Mus musculus
Manually annotated by BRENDA team
Wolosker, H.
Serine racemase and the serine shuttle between neurons and astrocytes
Biochim. Biophys. Acta
1814
1558-1566
2011
Mus musculus
Manually annotated by BRENDA team
Foltyn, V.N.; Zehl, M.; Dikopoltsev, E.; Jensen, O.N.; Wolosker, H.
Phosphorylation of mouse serine racemase regulates D-serine synthesis
FEBS Lett.
584
2937-2941
2010
Mus musculus
Manually annotated by BRENDA team
Ding, X.; Ma, N.; Nagahama, M.; Yamada, K.; Semba, R.
Localization of D-serine and serine racemase in neurons and neuroglias in mouse brain
Neurol. Sci.
32
263-267
2011
Mus musculus
Manually annotated by BRENDA team
Wolosker, H.; Mori, H.
Serine racemase: an unconventional enzyme for an unconventional transmitter
Amino Acids
43
1895-1904
2012
Mus musculus, Mus musculus C57BL/6
Manually annotated by BRENDA team
Balu, D.T.; Takagi, S.; Puhl, M.D.; Benneyworth, M.A.; Coyle, J.T.
D-Serine and serine racemase are localized to neurons in the adult mouse and human forebrain
Cell. Mol. Neurobiol.
34
419-435
2014
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
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
J. Chromatogr. B
879
3162-3168
2011
Homo sapiens, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Inoue, R.; Yoshihisa, Y.; Tojo, Y.; Okamura, C.; Yoshida, Y.; Kishimoto, J.; Luan, X.; Watanabe, M.; Mizuguchi, M.; Nabeshima, Y.; Hamase, K.; Matsunaga, K.; Shimizu, T.; Mori, H.
Localization of serine racemase and its role in the skin
J. Invest. Dermatol.
134
1618-1626
2014
Mus musculus, Mus musculus C57BL/6
Manually annotated by BRENDA team
Horio, M.; Kohno, M.; Fujita, Y.; Ishima, T.; Inoue, R.; Mori, H.; Hashimoto, K.
Role of serine racemase in behavioral sensitization in mice after repeated administration of methamphetamine
PLoS ONE
7
e35494
2012
Mus musculus
Manually annotated by BRENDA team
Uda, K.; Abe, K.; Dehara, Y.; Mizobata, K.; Edashige, Y.; Nishimura, R.; Radkov, A.D.; Moe, L.A.
Triple serine loop region regulates the aspartate racemase activity of the serine/aspartate racemase family
Amino Acids
49
1743-1754
2017
Acropora millepora, Crassostrea gigas (A0A0U5AKI6), Mus musculus, Mus musculus (Q9QZX7), Penaeus monodon (A0A0U4MRI4)
Manually annotated by BRENDA team
Talukdar, G.; Inoue, R.; Yoshida, T.; Ishimoto, T.; Yaku, K.; Nakagawa, T.; Mori, H.
Novel role of serine racemase in anti-apoptosis and metabolism
Biochim. Biophys. Acta
1861
3378-3387
2017
Mus musculus (Q9QZX7)
Manually annotated by BRENDA team
Canu, N.; Ciotti, M.T.; Pollegioni, L.
Serine racemase a key player in apoptosis and necrosis
Front. Synaptic Neurosci.
6
9
2014
Homo sapiens (Q9GZT4), Mus musculus (Q9QZX7)
Manually annotated by BRENDA team
Ito, T.; Hayashida, M.; Kobayashi, S.; Muto, N.; Hayashi, A.; Yoshimura, T.; Mori, H.
Serine racemase is involved in D-aspartate biosynthesis
J. Biochem.
160
345-353
2016
Mus musculus (Q9QZX7), Rattus norvegicus (Q76EQ0)
Manually annotated by BRENDA team
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