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Information on EC 5.1.1.18 - serine racemase and Organism(s) Homo sapiens and UniProt Accession Q9GZT4

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EC Tree
     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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Homo sapiens
UNIPROT: Q9GZT4
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
Synonyms
serine racemase, srace, t01h8.2, ser racemase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ser racemase
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-serine = D-serine
show the reaction diagram
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-alanine
D-alanine
show the reaction diagram
very low activity
-
-
r
L-aspartate
D-aspartate
show the reaction diagram
low activity
-
-
r
L-serine
D-serine
show the reaction diagram
L-threo-3-hydroxyaspartate
D-threo-3-hydroxyaspartate
show the reaction diagram
i.e. L-THA, Ser racemase shows activity toward D,L-THA and L-THA. D-THA cannot act as a substrate and/or inhibitor for the enzyme. The highest level of activity is detected with L-THA
-
-
r
rac-threo-3-hydroxyaspartate
D-threo-3-hydroxyaspartate
show the reaction diagram
i.e. L-THA, Ser racemase shows activity toward D,L-THA and L-THA. D-THA cannot act as a substrate and/or inhibitor for the enzyme. The highest level of activity is detected with L-THA
-
-
?
D-serine
L-serine
show the reaction diagram
-
-
-
-
r
L-serine
D-serine
show the reaction diagram
L-serine
pyruvate + NH3
show the reaction diagram
-
elimination reaction
-
-
?
L-serine-O-sulfate
O-sulfopyruvate + NH3
show the reaction diagram
-
elimination reaction
-
-
?
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-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
pyridoxal 5'-phosphate
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
activates
Ca2+
-
stimulation 5-7fold of the enzyme's elimination and racemization activities
Mn2+
-
stimulation 5-7fold of the enzyme's elimination and racemization activities
additional information
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(thiophen-3-yl)propanedioate
-
1,4-dihydronicotinamide mononucleotide
the NADH precursor exhibits a partial mixed-type inhibition. Docking simulations suggest that all 1,4-dihydronicotinamide derivatives bind at the interdimeric interface, with the ring positioned in an unoccupied site next to the ATP binding site
-
1-(4-acetamidoanilino)-1-oxopropan-2-yl 3-[(2-chlorophenyl)sulfanyl]propanoate
-
1-(4-ethoxyanilino)-1-oxopropan-2-yl 3-[(2-chlorophenyl)sulfanyl]propanoate
-
1-anilino-1-oxopropan-2-yl 3-[(2-chlorophenyl)sulfanyl]propanoate
-
2,2-dichloromalonate
2,2-difluoromalonate
-
2-(4-acetamidoanilino)-2-oxoethyl 3-(2-fluorophenoxy)propanoate
-
2-(4-acetamidoanilino)-2-oxoethyl 3-(phenylsulfanyl)propanoate
-
2-(4-acetamidoanilino)-2-oxoethyl 3-[(2-chlorophenyl)sulfanyl]propanoate
-
2-(4-acetamidoanilino)-2-oxoethyl 3-[(2-fluorophenyl)sulfanyl]propanoate
-
2-(4-acetamidoanilino)-2-oxoethyl 3-[(2-methoxyphenyl)sulfanyl]propanoate
-
2-(4-acetamidoanilino)-2-oxoethyl 3-[(3-methoxyphenyl)sulfanyl]propanoate
-
2-(4-acetamidoanilino)-2-oxoethyl 3-[(4-methoxyphenyl)sulfanyl]propanoate
-
2-(4-acetamidoanilino)-2-oxoethyl 4-(2-methoxyphenyl)butanoate
-
2-aminomalonate
-
2-carboxylmalonate
-
2-chloromalonate
-
2-fluoromalonate
-
2-Hydroxymalonate
-
2-nitromalonate
-
3-aminopropane-1,1,3-tricarboxylate
-
benzylpropanedioate
-
beta-NADH
reduced NADH inhibits the serine racemase, the inhibition is partial, the IC50 value is several-fold higher than the intracellular NADH concentrations. At saturating concentrations of NADH, ATP binds with a 2fold lower affinity and without co-operativity, suggesting ligand competition. But NADH also reduces the weak activity of human serine racemase in the absence of ATP, indicating an additional ATP-independent inhibition mechanism. The inhibitory determinant is the N-substituted 1,4-dihydronicotinamide ring. NAD+ does not seem to compete at all with NADH. Identification of the NADH-binding site, overview
beta-NADPH
-
bis(hydroxymethyl)propanedioate
-
butylpropanedioic acid
-
cyclobutane-1,1,3,3-tetracarboxylate
-
dimethylmalonate
-
ethane-1,1,2,2-tetracarboxylic acid
-
ethane-1,1,2-tricarboxylate
-
glycine
competitive inhibitor, the active site ligand glycine increases the enzyme's affinity for ATP by 22fold and abolishes cooperativity while ATP increases the noncooperative glycine binding 15fold. The in vivo concentration plays a role in D-serine synthesis (i.e., glycine concentration in astrocytes is in the 3-6 mM range)
L-aspartate
competitive
L-erythro-3-hydroxyaspartate
competitive versus L-serine
malonate
methylmalonate
-
N-(4-acetamidophenyl)-N2-[3-[(2-chlorophenyl)sulfanyl]propanoyl]alaninamide
-
N-(4-acetamidophenyl)-N2-[3-[(2-methoxyphenyl)sulfanyl]propanoyl]alaninamide
-
N-(4-acetylphenyl)-2-[(3,4-dichlorophenyl)acetyl]hydrazine-1-carboxamide
-
N-(4-bromophenyl)-N2-[(4-fluorophenoxy)acetyl]glycinamide
-
N2-[(4-bromophenoxy)acetyl]-N-(2,6-difluorophenyl)glycinamide
-
N2-[(4-bromophenoxy)acetyl]-N-(4-iodophenyl)glycinamide
-
N2-[(4-chlorophenoxy)acetyl]-N-(2,3,4-trifluorophenyl)glycinamide
-
N2-[(4-fluorophenoxy)acetyl]-N-(4-iodophenyl)glycinamide
-
oxirane-2,3-dicarboxylate
-
phosphatidylinositol-4,5-bisphosphate
-
propane-1,2,2,3-tetracarboxylate
-
S-nitrosoglutathione
GSNO, inhibition of human serine racemase by S-nitrosylation at Cys133, Cys128,and Cys269. The time-course is markedly biphasic, with a fast phase associated with the reaction of Cys113. The inhibition results from a conformational change rather than the direct displacement of ATP. Effect of nitrosylation on the cross-talk between ATP binding site and active site, both ATP and glycine bind to their respective sites with the same affinity regardless of the nitrosylation state
cystamine
-
abolishes the enzyme activity
glycine
-
-
L-erythro-3-hydroxyaspartate
-
-
malonate
-
-
nitric oxide
-
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,4-dithiothreitol
-
chemical reduction with DTT increases the enzyme activity by elevating Vmax
ATP
-
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
D-serine
-
up to 5fold increase in activity
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
-
glycine
-
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
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
16 - 54
L-serine
10.8
D-serine
-
pH 8.0
1 - 48
L-serine
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.85 - 2.77
L-serine
1.41
D-serine
-
pH 8.0
0.048 - 0.69
L-serine
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.016 - 0.17
L-serine
0.001 - 0.0042
L-serine
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.018
1,4-dihydronicotinamide mononucleotide
pH 8.0, 37°C
-
0.019
2,2-dichloromalonate
pH 8.0, 37°C
0.15
glycine
pH and temperature not specified in the publication
1.9
L-aspartate
pH and temperature not specified in the publication
0.049
L-erythro-3-hydroxyaspartate
pH and temperature not specified in the publication
0.366
glycine
-
-
0.011
L-erythro-3-hydroxyaspartate
-
-
0.033
malonate
-
-
additional information
additional information
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.243
beta-NADH
Homo sapiens
pH 8.0, 37°C
1.31
malonate
Homo sapiens
pH and temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.139
purified His-tagged wild-type enzyme, pH 8.0, 37°C, substrate D-serine
0.148
purified recombinant enzyme, L-Ser racemase activity, pH 8.0, 30°C
0.263
purified His-tagged wild-type enzyme, pH 8.0, 37°C, substrate L-serine
16.2
-
pH 8.0
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
-
assay at
9
-
about, elimination and racemization activities
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
neuronal like cell line
Manually annotated by BRENDA team
an astrocytoma cell line
Manually annotated by BRENDA team
-
increased expression in schizophrenia
Manually annotated by BRENDA team
-
high expression level, especially in neocortex and hippocampus
Manually annotated by BRENDA team
-
cell line U87, inverse regulation of enzyme activity by D-serine and nitric oxide
Manually annotated by BRENDA team
additional information
-
quantitative immunohistochemic analysis, overview
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
malfunction
physiological function
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
SRR_HUMAN
340
0
36566
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40000
-
2 * 40000, recombinant His-tagged enzyme, SDS-PAGE, the major oligomeric form of recombinant enzyme in aqueous solution. The enzyme is most active as a noncovalent dimer containing one or more free sulfhydryls in the enzymes active center or a modulatory site
87500
-
recombinant His-tagged enzyme, gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
36000-37000, calculated
homodimer
2 * 42000, native enzyme from brain, SDS-PAGE, 2 * 39000, recombinnat enzyme from HEK-293 cells, SDS-PAGE
monomer
crystal structure analysis, PDB ID 3L6B
?
-
x * 36000-37000
dimer
-
2 * 40000, recombinant His-tagged enzyme, SDS-PAGE, the major oligomeric form of recombinant enzyme in aqueous solution. The enzyme is most active as a noncovalent dimer containing one or more free sulfhydryls in the enzyme's active center or a modulatory site
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
S-nitrosylation
human serine racemase is nitrosylated at multiple sites, which inhibits the enzyme activity. Besides Cys113, two additional cysteine residues, Cys269, unique to the human orthologue, and Cys128, are recognized as S-nitrosylation sites through mass spectrometry and site-directed mutagenesis. S-nitrosylation produces a partial interruption of the cross-talk between the ATP binding site and the active site. The inhibition results from a conformational change rather than the direct displacement of ATP
nitrosylation
-
S-nitrosylation inhibits racemase activity
phosphoprotein
-
serine racemase can be activated by phosphorylation
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant mutant C2D/C6D by sitting drop vapor diffusion, 10 mg/ml protein in 20 mM Tris-HCl, pH 8.0, 100 mM NaCl, 10% glycerol, 0.05 mM PLP, 2 mM MgCl2, 5 mM dithiothreitol, mixed with 25% PEG 3350, 200 mM sodium malonate, and 50 mM MnCl2 as the reservoir solution, 4 days, the selenomethionine-labeled enzyme crystals grow under similar conditions, X-ray diffraction structure determination and analysis at 1.5-1.7 A resolution
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C113S
site-directed mutagenesis, the C113S mutant exhibits a KM for L-serine which is 3.5fold higher than for the wild-type enzyme and a 3.3fold lower specific activity. ATP binding to the mutant in the presence of L-serine occurs with a 5fold higher EC50 compared to wild-type, with conserved binding cooperativity. Phenotype, overview
C2D/C6D
site-directed mutagenesis
D318N
site-directed mutagenesis
S84A
site-directed mutagenesis, the mutant is inactive in L- or D-serine racemization, but still shows dehydration activity
additional information
-
generation of enzyme mutants by random mutagenesis for determination of structurally and functionally important residues in the enzyme, e.g. S84 and P111, that are crucial for enzyme activity, and C217 and K221 that are important for Mg2+ binding and enzyme stability
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
enzyme residues C217 and K221 are important for Mg2+ binding and enzyme stability
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant C-terminally His6-tagged wild-type and mutant enzymes from Escherichia coli strain MC1061 by nickel affinity chromatography and gel filtration
recombinant His-tagged enzyme from Escherichia coli nickel affinity chromatography and dialysis, to near homogeneity
recombinant His-tagged enzyme mutant from Escherichia coli strain Rosetta 2 (DE3) by affinity chromatography and gel filtration to over 98% purity
recombinant His-tagged wild-type enzyme from Escherichia coli strain BL21 CodonPlus (DE3)-RIL by nickel affinity chromatography
recombinant His6-tagged wild-type and mutant enzymes from Escherichia coli strain BL21 CodonPlus (DE3)-RIL
expression in Escherichia coli with N-terminal His-tag, purification protocol from inclusion bodies
-
recombinant enzyme
-
recombinant His-tagged enzyme from Escherichia coli strain BL21-CodonPlus(DE3)-RIL by metal affinity chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloning from genomic DNA, DNA and amino acid sequence determination
expression of C-terminally His6-tagged wild-type and mutant enzymes in Escherichia coli strain MC1061
expression of His-tagged enzyme mutant in Escherichia coli strain Rosetta 2 (DE3)
recombinant expression of His-tagged wild-type enzyme in Escherichia coli strain BL21 CodonPlus (DE3)-RIL
recombinant expression of N-terminally His-tagged enzyme in Escherichia coli
sequence comparisons, recombinant expression of His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21 CodonPlus (DE3)-RIL
enzyme expression of His-tagged enzyme in Escherichia coli strain BL21-CodonPlus(DE3)-RIL
-
expression of the highly active His-tagged serine racemase from brain in moderate halophilic bacteria, the recombinant enzyme shows 2.6fold higher elimination than racemization activity
-
optimization for expression in Escherichia coli
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the enzyme accumulates in the late pase of apoptosis. The increased enzyme expression is not dependent on the increased transcription or increased stability of serine racemase mRNA
the enzyme is downregulated in the early phase of neuronal apoptosis, but modulation of serine racemase expression by apoptosis is stimulus-dependent
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
pharmacology
because D-serine affects NMDAR signaling throughout the brain, serine racemase is a promising target for the treatment of disorders related to NMDAR dysfunction
drug development
-
serine racemase inhibitors might be useful in treatment of neurodegenrative diseases
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Xia, M.; Liu, Y.; Figueroa, D.J.; Chiu, C.S.; Wei, N.; Lawlor, A.M.; Lu, P.; Sur, C.; Koblan, K.S.; Connolly, T.M.
Characterization and localization of a human serine racemase
Brain Res. Mol. Brain Res.
125
96-104
2004
Homo sapiens (Q9GZT4), Homo sapiens
Manually annotated by BRENDA team
De Miranda, J.; Santoro, A.; Engelender, S.; Wolosker, H.
Human serine racemase: molecular cloning, genomic organization and functional analysis
Gene
256
183-188
2000
Homo sapiens (Q9GZT4), Homo sapiens
Manually annotated by BRENDA team
Shoji, K.; Mariotto, S.; Ciampa, A.R.; Suzuki, H.
Regulation of serine racemase activity by D-serine and nitric oxide in human glioblastoma cells
Neurosci. Lett.
392
75-78
2006
Homo sapiens
Manually annotated by BRENDA team
Nagayoshi, C.; Ishibashi, M.; Kita, Y.; Matsuoka, M.; Nishimoto, I.; Tokunaga, M.
Expression, refolding and characterization of human brain serine racemase in Escherichia coli with N-terminal His-tag
Protein Pept. Lett.
12
487-490
2005
Homo sapiens
Manually annotated by BRENDA team
Wu, S.; Basile, A.S.; Barger, S.W.
Induction of serine racemase expression and D-serine release from microglia by secreted amyloid precursor protein (sAPP)
Curr. Alzheimer Res.
4
243-251
2007
Rattus norvegicus, Homo sapiens (Q9GZT4)
Manually annotated by BRENDA team
Verrall, L.; Walker, M.; Rawlings, N.; Benzel, I.; Kew, J.N.; Harrison, P.J.; Burnet, P.W.
D-Amino acid oxidase and serine racemase in human brain: normal distribution and altered expression in schizophrenia
Eur. J. Neurosci.
26
1657-1669
2007
Homo sapiens
Manually annotated by BRENDA team
Steffek, A.E.; Haroutunian, V.; Meador-Woodruff, J.H.
Serine racemase protein expression in cortex and hippocampus in schizophrenia
NeuroReport
17
1181-1185
2006
Homo sapiens
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
Hoffman, H.; Jiraskova, J.; Zvelebil, M.; Konvalinka, J.
Random mutagenesis of human serine racemase reveals residues important for the enzymatic activity
Collect. Czech. Chem. Commun.
75
59-79
2010
Homo sapiens
-
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
Smith, M.A.; Mack, V.; Ebneth, A.; Moraes, I.; Felicetti, B.; Wood, M.; Schonfeld, D.; Mather, O.; Cesura, A.; Barker, J.
The structure of mammalian serine racemase: evidence for conformational changes upon inhibitor binding
J. Biol. Chem.
285
12873-12881
2010
Rattus norvegicus, Homo sapiens (Q9GZT4), Homo sapiens
Manually annotated by BRENDA team
Nagayoshi, C.; Ishibashi, M.; Tokunaga, M.
Purification and characterization of human brain serine racemase expressed in moderately halophilic bacteria
Protein Pept. Lett.
16
201-206
2009
Homo sapiens
Manually annotated by BRENDA team
Wang, W.; Barger, S.W.
Roles of quaternary structure and cysteine residues in the activity of human serine racemase
BMC Biochem.
12
63
2011
Homo sapiens
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
Marchetti, M.; Bruno, S.; Campanini, B.; Peracchi, A.; Mai, N.; Mozzarelli, A.
ATP binding to human serine racemase is cooperative and modulated by glycine
FEBS J.
280
5853-5863
2013
Homo sapiens
Manually annotated by BRENDA team
Campanini, B.; Spyrakis, F.; Peracchi, A.; Mozzarelli, A.
Serine racemase: a key player in neuron activity and in neuropathologies
Front. Biosci.
18
1112-1128
2013
Homo sapiens
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
Wang, C.Y.; Ku, S.C.; Lee, C.C.; Wang, A.H.
Modulating the function of human serine racemase and human serine dehydratase by protein engineering
Protein Eng. Des. Sel.
25
741-749
2012
Homo sapiens (Q9GZT4), Homo sapiens
Manually annotated by BRENDA team
Bruno, S.; Marchesani, F.; Dellafiora, L.; Margiotta, M.; Faggiano, S.; Campanini, B.; Mozzarelli, A.
Human serine racemase is allosterically modulated by NADH and reduced nicotinamide derivatives
Biochem. J.
473
3505-3516
2016
Homo sapiens (Q9GZT4), Homo sapiens
Manually annotated by BRENDA team
Nitoker, N.; Major, D.T.
Understanding the reaction mechanism and intermediate stabilization in mammalian serine racemase using multiscale quantum-classical simulations
Biochemistry
54
516-527
2015
Rattus norvegicus (Q76EQ0), Homo sapiens (Q9GZT4), Homo sapiens
Manually annotated by BRENDA team
Marchesani, F.; Bruno, S.; Paredi, G.; Raboni, S.; Campanini, B.; Mozzarelli, A.
Human serine racemase is nitrosylated at multiple sites
Biochim. Biophys. Acta
1866
813-821
2018
Homo sapiens (Q9GZT4), Homo sapiens
Manually annotated by BRENDA team
Mori, H.; Wada, R.; Li, J.; Ishimoto, T.; Mizuguchi, M.; Obita, T.; Gouda, H.; Hirono, S.; Toyooka, N.
In silico and pharmacological screenings identify novel serine racemase inhibitors
Bioorg. Med. Chem. Lett.
24
3732-3735
2014
Homo sapiens (Q9GZT4)
Manually annotated by BRENDA team
Takahara, S.; Nakagawa, K.; Uchiyama, T.; Yoshida, T.; Matsumoto, K.; Kawasumi, Y.; Mizuguchi, M.; Obita, T.; Watanabe, Y.; Hayakawa, D.; Gouda, H.; Mori, H.; Toyooka, N.
Design, synthesis, and evaluation of novel inhibitors for wild-type human serine racemase
Bioorg. Med. Chem. Lett.
28
441-445
2017
Homo sapiens (Q9GZT4), Homo sapiens
Manually annotated by BRENDA team
Vorlova, B.; Nachtigallova, D.; Jiraskova-Vanickova, J.; Ajani, H.; Jansa, P.; Rezac, J.; Fanfrlik, J.; Otyepka, M.; Hobza, P.; Konvalinka, J.; Lepsik, M.
Malonate-based inhibitors of mammalian serine racemase kinetic characterization and structure-based computational study
Eur. J. Med. Chem.
89
189-197
2015
Homo sapiens (Q9GZT4), Homo sapiens
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
Katane, M.; Saitoh, Y.; Uchiyama, K.; Nakayama, K.; Saitoh, Y.; Miyamoto, T.; Sekine, M.; Uda, K.; Homma, H.
Characterization of a homologue of mammalian serine racemase from Caenorhabditis elegans the enzyme is not critical for the metabolism of serine invivo
Genes Cells
21
966-977
2016
Caenorhabditis elegans (Q93968), Caenorhabditis elegans, Homo sapiens (Q9GZT4), Homo sapiens, Caenorhabditis elegans N2 (Q93968)
Manually annotated by BRENDA team