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beta-chloro-L-alanine
pyruvate + NH3 + ?
-
the artificial serine racemase substrate is degraded via alpha,beta-elimination
-
-
?
D-alanine
L-alanine
-
-
-
-
r
D-serine
S-serine
-
-
-
-
?
D-threonine
L-threonine
13% of the activity with L-serine
-
-
r
L-arginine
D-arginine
7% of the activity with L-serine
-
-
?
L-glutamine
D-glutamine
4.5% of the activity with L-serine
-
-
?
L-serine O-sulfate
O-sulfopyruvate + NH3
L-serine O-sulfate
pyruvate + NH3 + ?
-
the artificial serine racemase substrate is degraded via alpha,beta-elimination
-
-
?
L-serine-O-sulfate
O-sulfopyruvate + NH3
-
elimination reaction
-
-
?
L-threo-3-hydroxyaspartate
D-threo-3-hydroxyaspartate
L-threo-3-hydroxyaspartate
pyruvate + NH3 + ?
-
the artificial serine racemase substrate is degraded via alpha,beta-elimination
-
-
?
L-threonine
2-oxobutanoate + NH3
-
alpha,beta-elimination reaction
-
-
?
rac-threo-3-hydroxyaspartate
D-threo-3-hydroxyaspartate
additional information
?
-
D-serine
L-serine
-
-
-
-
r
D-serine
L-serine
-
-
-
r
D-serine
L-serine
-
-
-
-
r
D-serine
L-serine
-
racemization reaction
-
-
r
D-serine
L-serine
-
racemization reaction
-
-
r
D-serine
L-serine
38% of the activity with L-serine
-
-
r
D-serine
L-serine
-
-
-
-
?
D-serine
L-serine
-
-
-
-
r
D-serine
pyruvate + NH3
-
-
-
?
D-serine
pyruvate + NH3
-
-
-
-
?
D-serine
pyruvate + NH3
-
alpha,beta-elimination reaction
-
-
?
L-alanine
D-alanine
13% of the activity with L-serine
-
-
?
L-alanine
D-alanine
very low activity
-
-
r
L-alanine
D-alanine
very low activity
-
-
r
L-alanine
D-alanine
very low activity
-
-
r
L-alanine
D-alanine
-
-
-
-
r
L-aspartate
D-aspartate
low activity
-
-
r
L-aspartate
D-aspartate
low activity
-
-
r
L-aspartate
D-aspartate
low activity
-
-
r
L-aspartate
D-aspartate
-
-
-
r
L-aspartate
D-aspartate
enzyme SRR catalyses Asp racemization by a mechanism similar to Ser racemization. Lys56 performs the alpha-proton abstraction/donation of L-Asp and Ser84 is responsible for alpha-proton transferring for D-Asp
-
-
r
L-serine
D-serine
-
-
-
-
r
L-serine
D-serine
-
-
-
?
L-serine
D-serine
highly specific for
-
-
?
L-serine
D-serine
-
-
-
r
L-serine
D-serine
-
-
-
r
L-serine
D-serine
-
-
-
-
r
L-serine
D-serine
-
alanine racemase 2, Alr2, converts L-serine to an approximately equal amount of D-serine. When tested with D-serine, Alr2 does not convert as much, and nearly 75% of the D-serine remains in the D-form
-
-
r
L-serine
D-serine
-
-
-
-
r
L-serine
D-serine
-
alanine racemase 2, Alr2, converts L-serine to an approximately equal amount of D-serine. When tested with D-serine, Alr2 does not convert as much, and nearly 75% of the D-serine remains in the D-form
-
-
r
L-serine
D-serine
-
-
-
r
L-serine
D-serine
-
-
-
-
?
L-serine
D-serine
-
-
-
-
r
L-serine
D-serine
-
-
-
-
?
L-serine
D-serine
-
-
-
-
r
L-serine
D-serine
-
-
-
?
L-serine
D-serine
-
-
-
-
?
L-serine
D-serine
-
-
-
?
L-serine
D-serine
-
-
-
-
?
L-serine
D-serine
-
-
-
r
L-serine
D-serine
-
-
-
-
r
L-serine
D-serine
-
-
-
r
L-serine
D-serine
-
-
-
-
r
L-serine
D-serine
-
-
-
r
L-serine
D-serine
-
-
-
-
r
L-serine
D-serine
-
-
-
r
L-serine
D-serine
-
-
-
-
r
L-serine
D-serine
-
-
D-serine is an important modulator of the N-methyl-D-aspartate receptor function
-
?
L-serine
D-serine
-
racemization reaction
-
-
r
L-serine
D-serine
-
D-serine is an N-methyl-d-aspartate receptor co-agonist, synthesized by serine racemase and degraded by d-amino acid oxidase
-
-
?
L-serine
D-serine
-
the astrocytic enzyme synthesizes the N-methyl-D-aspartate receptor coagonist D-serine, and is involved in development of schizophrenia and glutamatergic dysfunction, astrocytes may play a direct role in N-methyl-D-aspartate receptor dysfunction in schizophrenia, overview
-
-
?
L-serine
D-serine
-
enzyme residues S84 and P111 are crucial for enzyme activity
-
-
?
L-serine
D-serine
-
-
-
r
L-serine
D-serine
-
-
662116, 679781, 681530, 703957, 705049, 705289, 706532, 714348, 716344, 726664, 727279, 728034 -
-
?
L-serine
D-serine
-
-
-
-
r
L-serine
D-serine
-
-
-
?
L-serine
D-serine
-
-
-
r
L-serine
D-serine
-
-
-
-
r
L-serine
D-serine
-
-
-
r
L-serine
D-serine
-
specific for synthesis of D-serine
-
?
L-serine
D-serine
-
-
D-serine is an important modulator of the N-methyl-D-aspartate receptor function
-
?
L-serine
D-serine
-
racemization reaction
-
-
r
L-serine
D-serine
D-serine is a coagonist with glutamate at NMDA receptors, postsynaptic stimulation of nitric-oxide formation feeds back to presynaptic cells to S-nitrosylate SR and decrease D-serine availability to postsynaptic NMDA receptors, enzyme regulation, mechanism, overview
-
-
?
L-serine
D-serine
-
developmental regulation of enzyme expression in neuronal ganglion cells of the retina, overview, D-serine is the endogenous ligand for the glycine modulatory binding site of the NMDA receptor
-
-
?
L-serine
D-serine
-
D-serine is stored primarily within astrocytes ensheathing neuronal synapses containing NMDA receptors, model of D-serine signalling in the brain, overview
-
-
?
L-serine
D-serine
enzyme SRR catalyses Ser racemization via a two-base mechanism in which two catalytic residues, Lys and Ser play vital roles in the abstraction and donation of alpha-proton of L-Ser and D-Ser, respectively
-
-
r
L-serine
D-serine
-
-
-
-
?
L-serine
D-serine
-
developmental regulation of enzyme expression in neuronal ganglion cells of the retina, overview, D-serine is the endogenous ligand for the glycine modulatory binding site of the NMDA receptor
-
-
?
L-serine
D-serine
-
-
-
-
?
L-serine
D-serine
-
-
D-serine is an important modulator of the N-methyl-D-aspartate receptor function
-
?
L-serine
D-serine
-
-
-
r
L-serine
D-serine
-
racemization reaction
-
-
r
L-serine
D-serine
SerR is highly specific for serine
-
-
r
L-serine
D-serine
-
-
-
r
L-serine
D-serine
-
-
-
r
L-serine
D-serine
the forward reaction is preferred, serine is preferred to threonine
-
-
r
L-serine
D-serine
-
-
-
-
?
L-serine
D-serine
-
-
-
-
r
L-serine
D-serine
-
-
-
?
L-serine
D-serine
-
-
-
r
L-serine
D-serine
-
-
highly selctive toward L-serine
-
?
L-serine
D-serine
-
D-serine is an endogenous N-methyl-D-aspartate, NMDA, receptor coagonist
-
?
L-serine
D-serine
D-serine, an endogenous co-agonist of N-methyl-D-aspartate receptors in vertebrate retina, modulates glutamate sensitivity of retinal neurons, overview
-
-
?
L-serine
D-serine
-
mechanisms regulating D-serine production by the enzyme serine racemase via translocation from cytosol to membranes, overview
D-serine is a physiological coagonist of N-methyl D-aspartate receptors, NMDARs, that plays a major role in several NMDAR-dependent events
-
?
L-serine
D-serine
-
-
-
r
L-serine
D-serine
Roseobacter litoralis ATCC 49566 / DSM 6996 / JCM 21268 / NBRC 15278 / OCh 149
-
-
-
r
L-serine
D-serine
-
-
-
-
?
L-serine
D-serine
-
-
-
?
L-serine
D-serine
-
-
-
r
L-serine
D-serine
on binding of the substrate, the small domain rotates toward the large domain to close the active site, substrate binding structure, Lys57 is the catalytic residue of the wild-type enzyme, overview
-
-
r
L-serine
D-serine
-
-
-
-
r
L-serine
D-serine
-
-
-
r
L-serine
pyruvate + NH3
-
elimination reaction
-
-
?
L-serine
pyruvate + NH3
-
-
-
-
?
L-serine
pyruvate + NH3
-
-
-
?
L-serine
pyruvate + NH3
-
-
-
-
?
L-serine
pyruvate + NH3
-
alpha,beta-elimination reaction
-
-
?
L-serine O-sulfate
O-sulfopyruvate + NH3
-
-
-
-
?
L-serine O-sulfate
O-sulfopyruvate + NH3
-
-
-
?
L-threo-3-hydroxyaspartate
D-threo-3-hydroxyaspartate
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
L-threo-3-hydroxyaspartate
D-threo-3-hydroxyaspartate
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
L-threonine
D-threonine
-
-
-
r
L-threonine
D-threonine
the forward reaction is preferred, serine is preferred to threonine
-
-
r
L-threonine
D-threonine
40% of the activity with L-serine
-
-
r
rac-threo-3-hydroxyaspartate
D-threo-3-hydroxyaspartate
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
-
-
?
rac-threo-3-hydroxyaspartate
D-threo-3-hydroxyaspartate
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
-
-
?
additional information
?
-
-
enzyme product may serve as a ligand for setting the sensitivity of N-methyl-D-aspartate receptors under physiological conditions
-
-
?
additional information
?
-
the bifunctional enzyme catalyzes not only serine racemization but also dehydration of serine to pyruvate
-
-
?
additional information
?
-
-
the bifunctional enzyme catalyzes not only serine racemization but also dehydration of serine to pyruvate
-
-
?
additional information
?
-
the enzyme does not appear to metabolize D- and L-Ser in vivo
-
-
?
additional information
?
-
-
the enzyme does not appear to metabolize D- and L-Ser in vivo
-
-
?
additional information
?
-
the recombinant enzyme T01H8.2 expressed in Escherichia coli exhibits Ser racemase activity in addition to low, but detectable, Asp and Ala racemase activities in vitro. T01H8.2 shows dehydratase activity toward several hydroxyamino acids in addition to racemase activity. The enzyme does not appear to metabolize D- and L-Ser in vivo. Substrate specificity, overview. No activity on L-Glu
-
-
?
additional information
?
-
-
the recombinant enzyme T01H8.2 expressed in Escherichia coli exhibits Ser racemase activity in addition to low, but detectable, Asp and Ala racemase activities in vitro. T01H8.2 shows dehydratase activity toward several hydroxyamino acids in addition to racemase activity. The enzyme does not appear to metabolize D- and L-Ser in vivo. Substrate specificity, overview. No activity on L-Glu
-
-
?
additional information
?
-
the enzyme does not appear to metabolize D- and L-Ser in vivo
-
-
?
additional information
?
-
the recombinant enzyme T01H8.2 expressed in Escherichia coli exhibits Ser racemase activity in addition to low, but detectable, Asp and Ala racemase activities in vitro. T01H8.2 shows dehydratase activity toward several hydroxyamino acids in addition to racemase activity. The enzyme does not appear to metabolize D- and L-Ser in vivo. Substrate specificity, overview. No activity on L-Glu
-
-
?
additional information
?
-
-
the enzyme catalyzes racemization and dehydration of both isomers of serine
-
-
?
additional information
?
-
specific for L-serine
-
-
?
additional information
?
-
-
specific for L-serine
-
-
?
additional information
?
-
-
enzyme additionally catalyzes elimination reaction of D-/L-serine and of L-serine-O-sulfate
-
-
?
additional information
?
-
-
the enzyme also performs an elimination reaction
-
-
?
additional information
?
-
-
serine racemase is the pyridoxal 5'-phosphate-dependent enzyme that catalyzes L-serine racemisation to D-serine, and L- and D-serine beta-elimination in mammalian brain
-
-
?
additional information
?
-
-
the enzyme binds to the glutamate receptor interacting protein, to protein interacting with C kinase 1, and Golgi-localized protein Golga 3
-
-
?
additional information
?
-
analysis of enzyme-substrate-cofactor interactions in the active site, overview
-
-
?
additional information
?
-
-
analysis of enzyme-substrate-cofactor interactions in the active site, overview
-
-
?
additional information
?
-
reactions catalyzed by serine racemase are racemization and alpha,beta-elimination, mechanisms, overview
-
-
?
additional information
?
-
the recombinant enzyme expressed in Escherichia coli exhibits Ser racemase activity in addition to low, but detectable, Asp and Ala racemase activities in vitro. T01H8.2 shows dehydratase activity toward several hydroxyamino acids in addition to racemase activity. Substrate specificity, overview. No activity on L-Glu
-
-
?
additional information
?
-
-
the recombinant enzyme expressed in Escherichia coli exhibits Ser racemase activity in addition to low, but detectable, Asp and Ala racemase activities in vitro. T01H8.2 shows dehydratase activity toward several hydroxyamino acids in addition to racemase activity. Substrate specificity, overview. No activity on L-Glu
-
-
?
additional information
?
-
the bifunctional enzyme catalyzes not only serine racemization but also dehydration of serine to pyruvate
-
-
?
additional information
?
-
-
the bifunctional enzyme catalyzes not only serine racemization but also dehydration of serine to pyruvate
-
-
?
additional information
?
-
-
enzyme modulates physiologic regulation of cerebellar granule cell migration
-
-
?
additional information
?
-
-
enzyme product may serve as a ligand for setting the sensitivity of N-methyl-D-aspartate receptors under physiological conditions
-
-
?
additional information
?
-
-
main enzyme to synthesize D-serine
-
-
?
additional information
?
-
racemization and elimination activities reside at the same active site of enzyme. Racemization activity is specific to serine, elimination activity has a broader specificity for L-amino acids with a suitable leaving group at the beta-carbon
-
-
?
additional information
?
-
-
racemization and elimination activities reside at the same active site of enzyme. Racemization activity is specific to serine, elimination activity has a broader specificity for L-amino acids with a suitable leaving group at the beta-carbon
-
-
?
additional information
?
-
-
ratio of elimination reaction/racemization reaction for substrate L-serine is 3.7
-
-
?
additional information
?
-
-
ratio of synthesized pyruvate/D-serine is about 3
-
-
?
additional information
?
-
-
serine racemase is the major enzyme for D-serine production in the brain, D-serine is the predominant endogenous coagonist of the NMDA receptor in the forebrain, and D-serine may be involved in controlling the extent of NMDA receptor-mediated neurotoxic insults observed in disorders including Alzheimers disease.
-
-
?
additional information
?
-
-
enzyme additionally catalyzes eleimination reaction of D-/L-serine and of L-serine-O-sulfate
-
-
?
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
-
-
?
additional information
?
-
enzyme SRR recognizes L-Asp as an in vivo substrate in addition to L- and D-Ser
-
-
?
additional information
?
-
reactions catalyzed by serine racemase are racemization and alpha,beta-elimination, mechanisms, overview
-
-
?
additional information
?
-
the enzyme has two enzymatic activities, namely, racemization and alpha,beta-elimination
-
-
?
additional information
?
-
wild-type enzyme SRR and SRR mutant S84A show Ser dehydratase activity. SRR-catalysed Asp racemization is less efficient and 550fold lower than that of Ser racemization
-
-
?
additional information
?
-
in addition to a serine racemase reaction, SerR catalyzes D- and L-serine dehydratase reactions, where the two compounds are converted to pyruvate, overview
-
-
?
additional information
?
-
-
in addition to a serine racemase reaction, SerR catalyzes D- and L-serine dehydratase reactions, where the two compounds are converted to pyruvate, overview
-
-
?
additional information
?
-
-
serine racemase is a bifunctional enzyme with racemase and dehydratase activities towards D- and L-serine
-
-
?
additional information
?
-
-
substrate specificity, the bifunctional enzyme shows high L-serine/L-threonine dehydratase activity, overview
-
-
?
additional information
?
-
substrate specificity, the bifunctional enzyme shows high L-serine/L-threonine dehydratase activity, overview
-
-
?
additional information
?
-
-
enzyme product may serve as a ligand for setting the sensitivity of N-methyl-D-aspartate receptors under physiological conditions
-
-
?
additional information
?
-
-
role for D-serine in peripheral nerve transduction
-
-
?
additional information
?
-
-
serine racemase may negatively regulate cellular differentiation through the inhibition of sry-typeHMGbox 9, i.e.Sox9 transcriptional activity in chondrocytes
-
-
?
additional information
?
-
regulation of the D-serine content in the forebrain and in C6 glioma cells, that lack the main degerative enzyme D-amino acid oxidase, might act via mechanisms including SRR operating in alpha,beta-eliminase mode, converting D-serine to pyruvate, and regulation by serine transport, in which the alanine-serine-cysteine transporter ASCT2 is implicated, overview. D-serine transport mediated by ASCT2 contributes prominently to D-serine homeostasis when DAO activity is absent
-
-
?
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
-
-
?
additional information
?
-
analysis of enzyme-substrate-cofactor interactions in the active site, overview
-
-
?
additional information
?
-
the recombinant enzyme RiSR exhibits both racemization and dehydration activities exclusively towards serine. The catalytic efficiency for L-serine racemization of RiSR is 34fold higher than that of L-serine dehydration. RiSR primarily catalyses serine racemization rather than dehydration. The kcat/Km ratios of D-/L-serine and the racemization/dehydration ratio for RiSR are 0.95/1.01 and 34.4/38.3, respectively
-
-
?
additional information
?
-
Roseobacter litoralis ATCC 49566 / DSM 6996 / JCM 21268 / NBRC 15278 / OCh 149
the recombinant enzyme RiSR exhibits both racemization and dehydration activities exclusively towards serine. The catalytic efficiency for L-serine racemization of RiSR is 34fold higher than that of L-serine dehydration. RiSR primarily catalyses serine racemization rather than dehydration. The kcat/Km ratios of D-/L-serine and the racemization/dehydration ratio for RiSR are 0.95/1.01 and 34.4/38.3, respectively
-
-
?
additional information
?
-
the enzyme also catalyzes the dehydration of D- and L-serine resulting in pyruvate
-
-
?
additional information
?
-
-
the enzyme also catalyzes the dehydration of D- and L-serine resulting in pyruvate
-
-
?
additional information
?
-
-
the enzyme catalyzes both the racemization and alpha,beta-elimination reaction of L- and D-serine to yield pyruvate and ammonia
-
-
?
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(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-(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
-
3-aminopropane-1,1,3-tricarboxylate
-
Acetohydroxamic acid
-
i.e. Lithostat
adipodihydroxamic acid
-
-
alpha-(hydroxymethyl)-L-serine
-
substrate-product analogue, a modest, linear mixed-type inhibitor of serine racemase
aminooxyacetic acid
-
non-selective inhibitor
AMP-PCP
Mg-AMP-PCP is bound to the groove formed at the intersection between the domain interface and the subunit interface, structure and binding mode, overview. The binding of Mg-AMP-PCP to the enzyme in the open form does not induce a subunit conformational change, but, interestingly, changes the relative orientation between the two subunits
beta-chloro-L-alanine
-
2 mM, 68% residual activity
beta-fluoro-D,L-alanine
-
2 mM, 81% residual activity
beta-haloalanine
reacts with pyridoxal 5'-phosphate to yield thiazolidine derivative
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
bis(hydroxymethyl)propanedioate
-
cyclobutane-1,1,3,3-tetracarboxylate
-
cysteine
reacts with pyridoxal 5'-phosphate to yield thiazolidine derivative
D-cycloserine
-
2 mM, 64% inhibition
D-cysteine
-
2 mM, 72% residual activity
DL-Serine hydroxamate
-
-
DL-Threonine hydroxamate
-
-
ethane-1,1,2,2-tetracarboxylic acid
-
ethane-1,1,2-tricarboxylate
-
glutarodihydroxamic acid
-
-
homocysteine
reacts with pyridoxal 5'-phosphate to yield thiazolidine derivative
L-2,3-diaminopropionic acid
-
2 mM, 68% residual activity
L-aspartic acid beta-hydroxamate
-
a competitive and selective serine racemase inhibitor
L-Cycloserine
-
10 mM, 45% inhibition
L-erythro-3-hydroxyaspartate
L-homocysteic acid
-
2 mM, 59% residual activity
malonodihydroxamic acid
-
-
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
-
oxaloacetic acid
-
2 mM, 56% residual activity
oxalodihydroxamic acid
-
-
oxirane-2,3-dicarboxylate
-
phenazine
-
non-selective inhibitor
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
Sodium borohydride
complete inhibition at 1 mM
suberodihydroxamic acid
-
-
succinodihydroxamic acid
-
-
vorinostat
-
i.e. Zolinza
2,2-dichloromalonate
as malonate, it binds in a small pocket of the active site
amino-oxyacetic acid
complete inhibition
ATP
ATP decreases the serine racemase activity of SerR but increases the serine dehydratase activity
ATP
10-20% inhibition; 10-20% inhibition at 0.1-1 mM
Cu2+
-
cystamine
-
abolishes the enzyme activity
cystamine
-
50% inhibition at 0.0081 mM
EDTA
-
EDTA
-
non-selective inhibitor
EDTA
abolishes racemization and dehydration activites of the enzyme
Fe2+
complete inhibition of racemase activity at 1 mM
Fe2+
slight inhibition of both activities
Fe2+
20-30% inhibition; 20-30% inhibition
glycine
-
-
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)
glycine
-
2 mM, 20% residual activity
glycine
-
non-selective inhibitor
hydroxylamine
-
hydroxylamine
complete inhibition at 1 mM
L-asparagine
-
L-asparagine
-
2 mM, 38% residual activity
L-asparagine
-
non-selective inhibitor
L-aspartate
competitive
L-aspartic acid
-
2 mM, 53% residual activity
L-cysteine
-
2 mM, 58% residual activity
L-cysteine
-
10 mM, 90% inhibition
L-erythro-3-hydroxyaspartate
-
-
L-erythro-3-hydroxyaspartate
competitive versus L-serine
L-erythro-3-hydroxyaspartate
-
L-erythro-3-hydroxyaspartate
-
-
L-erythro-3-hydroxyaspartate
-
non-selective inhibitor
L-serine-O-sulfate
-
2 mM, 9% residual activity
L-serine-O-sulfate
-
10 mM, 50% inhibition
malonate
-
-
malonate
-
non-selective inhibitor
Ni2+
-
Ni2+
slight inhibition of both activities
nitric oxide
-
-
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
phosphatidylinositol-4,5-bisphosphate
-
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
phosphatidylinositol-4,5-bisphosphate
-
-
Zn2+
-
additional information
no inhibition by EDTA of the racemase activity
-
additional information
-
no inhibition by EDTA of the racemase activity
-
additional information
EDTA has no significant effect on enzyme activity. No inhibition by D-threo-3-hydroxyaspartate
-
additional information
-
EDTA has no significant effect on enzyme activity. No inhibition by D-threo-3-hydroxyaspartate
-
additional information
-
no effect by EDTA
-
additional information
-
S-nitrosylation or membrane binding inhibit racemase activity
-
additional information
design of high-affinity serine racemase effectors to finely modulate D-serine homeostasis; no enzyme inhibition by ADP and the oxidized forms NAD+ and NADP+. Molecular modeling. The NADH/NAD+ fragments 1-methyl-1,4-dihydronicotinamide (MNA-red), 1,4-dihydronicotinamide mononucleotide (NMN-red), their oxidized forms 1-methylnicotinamide (MNA-ox) and beta-nicotinamide monucleotide (NMN-ox), the fully reduced form of MNA-ox-1-methyl 3-piperidinecarboxamide (MPCA), ADP and diphosphate are screened at 2 mM concentration using the beta-elimination (EC 4.3.1.17) assay to identify the inhibitory determinant of NADH, inhibition mechanism, overview
-
additional information
-
design of high-affinity serine racemase effectors to finely modulate D-serine homeostasis; no enzyme inhibition by ADP and the oxidized forms NAD+ and NADP+. Molecular modeling. The NADH/NAD+ fragments 1-methyl-1,4-dihydronicotinamide (MNA-red), 1,4-dihydronicotinamide mononucleotide (NMN-red), their oxidized forms 1-methylnicotinamide (MNA-ox) and beta-nicotinamide monucleotide (NMN-ox), the fully reduced form of MNA-ox-1-methyl 3-piperidinecarboxamide (MPCA), ADP and diphosphate are screened at 2 mM concentration using the beta-elimination (EC 4.3.1.17) assay to identify the inhibitory determinant of NADH, inhibition mechanism, overview
-
additional information
in silico and pharmacological inhibitor screenings, enzyme homology modeling, four active sites of hSR (two malonate-bound and two ligand-free forms) are used in this protein structure-based virtual screening, ligand docking
-
additional information
design, synthesis, and evaluation of inhibitors for wild-type human serine racemase. Serine racemase inhibitors are therapeutic candidates for the treatment of neurodegenerative disorders and epileptic states. No inhibition by 2-(4-acetamidoanilino)-2-oxoethyl 3-[(3-chlorophenyl)sulfanyl]propanoate, N-[2-(4-acetamidoanilino)-2-oxoethyl]-3-[(2-chlorophenyl)sulfanyl]propanamide, N-[2-(4-acetamidoanilino)-2-oxoethyl]-3-[(2-methoxyphenyl)sulfanyl]propanamide, and N-(4-acetamidophenyl)-7-(2-methoxyphenyl)-4-oxoheptanamide
-
additional information
-
design, synthesis, and evaluation of inhibitors for wild-type human serine racemase. Serine racemase inhibitors are therapeutic candidates for the treatment of neurodegenerative disorders and epileptic states. No inhibition by 2-(4-acetamidoanilino)-2-oxoethyl 3-[(3-chlorophenyl)sulfanyl]propanoate, N-[2-(4-acetamidoanilino)-2-oxoethyl]-3-[(2-chlorophenyl)sulfanyl]propanamide, N-[2-(4-acetamidoanilino)-2-oxoethyl]-3-[(2-methoxyphenyl)sulfanyl]propanamide, and N-(4-acetamidophenyl)-7-(2-methoxyphenyl)-4-oxoheptanamide
-
additional information
malonate-based inhibitors of mammalian serine racemase, kinetic characterization and structure-based computational study. Enzyme-inhibitor structure-activity relationship. Ligand docking into the human enzyme active site with three thermodynamically favourable water molecules is able to discern qualitatively between good and weak inhibitors. Further improvement in ranking is obtained using advanced PM6-D3H4X/COSMO semiempirical quantum mechanics-based scoring which distinguishes between the compounds with IC50 better/worse than 2 mM, molecular dynamics, method, overview
-
additional information
-
malonate-based inhibitors of mammalian serine racemase, kinetic characterization and structure-based computational study. Enzyme-inhibitor structure-activity relationship. Ligand docking into the human enzyme active site with three thermodynamically favourable water molecules is able to discern qualitatively between good and weak inhibitors. Further improvement in ranking is obtained using advanced PM6-D3H4X/COSMO semiempirical quantum mechanics-based scoring which distinguishes between the compounds with IC50 better/worse than 2 mM, molecular dynamics, method, overview
-
additional information
EDTA impairs only the alpha,beta-elimination reaction, not the racemization. Several dicarboxylic acids are strong, competitive inhibitors of the enzyme
-
additional information
EDTA has no significant effect on enzyme activity. No inhibition by D-threo-3-hydroxyaspartate
-
additional information
-
EDTA has no significant effect on enzyme activity. No inhibition by D-threo-3-hydroxyaspartate
-
additional information
no inhibition by EDTA of the racemase activity
-
additional information
-
no inhibition by EDTA of the racemase activity
-
additional information
-
small aliphatic hydroxamic acids as potent serine racemase inhibitors, interaction with the pyridoxal-5'-phosphate cofactor, mechanistic analysis, overview. Some of these hydroxamic acids can act as nonspecific inhibitors of pyridoxal 5'-phosphate-dependent enzymes, the nonspecific effect is likely due to irreversible interaction of the hydroxamic acid moiety with pyridoxal 5'-phosphate to form aldoxime species
-
additional information
-
S-nitrosylation or membrane binding inhibit racemase activity
-
additional information
EDTA impairs only the alpha,beta-elimination reaction, not the racemization. Several dicarboxylic acids are strong, competitive inhibitors of the enzyme
-
additional information
Asp racemization is inhibited by EDTA and hydroxylamine
-
additional information
SerR was inhibited by pyridoxal 5'-phosphate-enzyme inhibitors
-
additional information
-
SerR was inhibited by pyridoxal 5'-phosphate-enzyme inhibitors
-
additional information
-
no inhibition by p-chloromercuribenzoate, iodoacetamide, and iodoacetate
-
additional information
no inhibition by p-chloromercuribenzoate, iodoacetamide, and iodoacetate
-
additional information
-
no inhibition by Triton X-100. Association of serine racemase to brain membranes inhibits D-serine synthesis. Feedback inactivation of D-serine synthesis by NMDA receptor-elicited translocation of serine racemase to the membrane, and this effect is averted by blockade of NMDA receptors
-
additional information
-
S-nitrosylation or membrane binding inhibit racemase activity
-
additional information
-
substrate-product analogue inhibitors of racemases may only be effective when the active site is capacious and/or plastic, or when the inhibitor is sufficiently flexible
-
additional information
-
not inhibitory: D-cycloserine
-
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0.49
L-serine O-sulfate
pH 8.0, 37°C, presence of 1 mM ATP, elimination reaction
additional information
additional information
-
2 - 3
D-serine
-
wild type enzyme, in the absence of Mg2+, pH and temperature not specified in the publication
3.2
D-serine
pH 8.0, 37°C, presence of 1 mM ATP, elimination reaction
8
D-serine
-
wild-type, racemization, pH 7.4, 37°C
8.2
D-serine
-
wild-type, racemization, presence of ATP, pH 7.4, 37°C
8.48
D-serine
-
pH 8.0, 30°C, recombinant wild-type enzyme
8.9
D-serine
-
wild type enzyme, in the presence of 1 mM Mg2+, pH and temperature not specified in the publication
9.2
D-serine
-
mutant Q155D, racemization, pH 7.4, 37°C
9.2
D-serine
-
mutant Q155D, racemization, presence of ATP, pH 7.4, 37°C
12.7
D-serine
pH 8.0, 30°C, recombinant mutant P150S/P151S/Y152S
14.5
D-serine
pH 8.0, 37°C, presence of 1 mM ATP, racemization reaction
20.9
D-serine
pH 8.0, 30°C, recombinant wild-type enzyme
21.4
D-serine
-
pH 8.0, 30°C, recombinant mutant P151S/F152S
28.9
D-serine
-
pH 8.0, 30°C, recombinant mutant P150S/P151S/F152S
28.9
D-serine
pH 8.0, 30°C, recombinant mutant P151S
29.3
D-serine
pH 8.0, 30°C, recombinant wild-type enzyme
36.8
D-serine
pH 8.0, 30°C, recombinant His-tagged enzyme
37.4
D-serine
pH 8.0, 30°C, recombinant mutant H150S
40
D-serine
-
mutant enzyme E219A/D225A, in the absence of Mg2+, pH and temperature not specified in the publication
44.1
D-serine
pH 8.0, 30°C, recombinant mutant H150S/P151S
45.1
D-serine
pH 8.0, 30°C, recombinant mutant N152S
48
D-serine
-
mutant enzyme E219A/D225A, in the presence of 1 mM Mg2+, pH and temperature not specified in the publication
49
D-serine
pH 8.0, 37°C, racemization reaction
55.2
D-serine
pH 8.0, 30°C, recombinant mutant H150S/N152S
60
D-serine
-
pH 8.0, 37°C
69.7
D-serine
pH 8.0, 30°C, recombinant mutant P151S/N152S
75
D-serine
pH 8.0, 37°C, elimination reaction
95.4
D-serine
pH 8.2, 95°C
119
D-serine
pH 8.0, 30°C, recombinant wild-type enzyme
172
D-serine
pH 8.0, 30°C, recombinant mutant H150S/P151S/N152S
252
D-serine
pH 8.0, 30°C, recombinant mutant H150S/P151S/F152S
1 - 4
L-serine
-
pH 8.0, 37°C, recombinant enzyme
1.8
L-serine
-
racemization reaction, isoform A, pH 8.6, 37°C
3.8
L-serine
pH 8.0, 37°C, recombinant wild-type enzyme
3.8
L-serine
pH 8.0, 37°C, presence of 1 mM ATP, racemization reaction
4
L-serine
pH 8.0, 37°C, presence of 1 mM ATP, elimination reaction
4.8
L-serine
-
pH 8.1, 37°C
6.12
L-serine
recombinant enzyme, pH 8.0, 30°C
7.71
L-serine
-
pH 8.0, 30°C, recombinant wild-type enzyme
9
L-serine
-
wild-type, racemization, pH 7.4, 37°C
9
L-serine
-
wild-type, racemization, presence of ATP, pH 7.4, 37°C
10
L-serine
-
pH 8.0, 37°C
10
L-serine
-
mutant Q155D, racemization, pH 7.4, 37°C
10
L-serine
-
wild type enzyme, in the presence of 1 mM Mg2+, pH and temperature not specified in the publication
10.5
L-serine
-
mutant Q155D, racemization, presence of ATP, pH 7.4, 37°C
13
L-serine
-
racemization reaction, isoform A, presence of ATP, pH 8.6, 37°C
14
L-serine
-
pH 7.5, 37°C, recombinant wild-type enzyme
14.9
L-serine
pH 8.0, 30°C, recombinant wild-type enzyme
15.1
L-serine
pH 8.0, 30°C, recombinant mutant P150S/P151S/Y152S
16
L-serine
pH 8.0, 37°C, recombinant wild-type enzyme
17
L-serine
-
pH 7.5, 37°C, recombinant mutant K39A
18
L-serine
-
wild type enzyme, in the absence of Mg2+, pH and temperature not specified in the publication
18
L-serine
pH 8.0, 30°C, recombinant mutant N152S
19
L-serine
-
pH and temperature not specified in the publication
19.2
L-serine
-
pH 8.0, 30°C, recombinant mutant P150S/P151S/F152S
21.5
L-serine
pH 8.0, 30°C, recombinant wild-type enzyme
30
L-serine
pH 8.0, 37°C, racemization reaction
30
L-serine
pH 8.0, 30°C, recombinant mutant P151S
38.1
L-serine
pH 8.0, 30°C, recombinant mutant P151S/N152S
39
L-serine
pH 8.0, 30°C, recombinant His-tagged enzyme
40
L-serine
-
in presence of ATP, pH 8.0, 37°C
42.4
L-serine
pH 8.0, 30°C, recombinant mutant H150S
42.6
L-serine
-
pH 8.0, 30°C, recombinant mutant P151S/F152S
48
L-serine
-
in absence of ATP, pH 8.0, 37°C
50
L-serine
pH 8.0, 37°C, recombinant mutant D318N
50.6
L-serine
pH 8.0, 30°C, recombinant mutant H150S/P151S
53.4
L-serine
pH 8.0, 30°C, recombinant mutant H150S/P151S/N152S
54
L-serine
pH 8.0, 37°C, recombinant mutant C113S
69.9
L-serine
pH 8.0, 30°C, recombinant mutant H150S/N152S
75
L-serine
pH 8.0, 37°C, elimination reaction
78
L-serine
-
mutant enzyme E219A/D225A, in the presence of 1 mM Mg2+, pH and temperature not specified in the publication
125
L-serine
pH 8.0, 30°C, recombinant mutant H150S/P151S/F152S
130
L-serine
-
mutant enzyme E219A/D225A, in the absence of Mg2+, pH and temperature not specified in the publication
146
L-serine
pH 8.0, 30°C, recombinant wild-type enzyme
185
L-serine
pH 8.2, 95°C
additional information
additional information
-
-
-
additional information
additional information
kinetic analysis
-
additional information
additional information
-
kinetic analysis
-
additional information
additional information
kinetic analysis
-
additional information
additional information
kinetics of wild-type and mutant enzymes
-
additional information
additional information
-
kinetics of wild-type and mutant enzymes
-
additional information
additional information
kinetics of the bifunctional enzyme, overview
-
additional information
additional information
-
kinetics of the bifunctional enzyme, overview
-
additional information
additional information
-
the enzyme shows no allosteric properties, it is not affected by either L-isoleucine or L-valine, or most of the metal ions
-
additional information
additional information
the enzyme shows no allosteric properties, it is not affected by either L-isoleucine or L-valine, or most of the metal ions
-
additional information
additional information
-
enzyme shows no allosteric properties
-
additional information
additional information
enzyme shows no allosteric properties
-
additional information
additional information
-
Michaelis-Menten kinetic analysis
-
additional information
additional information
-
Michaelis-Menten kinetics, kinetics of serine racemase alpha- and beta-elimination activities, overview
-
additional information
additional information
-
steady-state kinetics of wild-type and mutant enzymes for serine dehydration activity, EC 4.3.1.17, overview
-
additional information
additional information
kinetic parameters of Ser dehydratase activity and Asp racemase activity of wild-type and mutant enzymes
-
additional information
additional information
Lineweaver-Burk kinetics
-
additional information
additional information
-
Lineweaver-Burk kinetics
-
additional information
additional information
Lineweaver-Burk kinetics
-
additional information
additional information
Lineweaver-Burk kinetics
-
additional information
additional information
-
Lineweaver-Burk kinetics
-
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evolution
-
the eukaryotic serine racemase from Dictyostelium discoideum is a fold-type II pyridoxal 5'-phosphate-dependent enzyme
evolution
SerRs and AspRs are not separated by their racemase functions and form a serine/aspartate racemase family cluster based on phylogenetic analysis
evolution
SerRs and AspRs are not separated by their racemase functions and form a serine/aspartate racemase family cluster based on phylogenetic analysis, the organism has two paralogous genes, SerR and AspR. The presence of the triple serine loop region in both AspRs and SerRs leads to greater AspR activity while removing the triple serine loop region results in almost complete loss of AspR activity
evolution
SerRs and AspRs are not separated by their racemase functions and form a serine/aspartate racemase family cluster based on phylogenetic analysis, the organism has two paralogous genes, SerR and AspR. The presence of the triple serine loop region in both AspRs and SerRs leads to greater AspR activity while removing the triple serine loop region results in almost complete loss of AspR activity
evolution
-
SerRs and AspRs are not separated by their racemase functions and form a serine/aspartate racemase family cluster based on phylogenetic analysis, the organism has two paralogous genes, SerR and AspR. The presence of the triple serine loop region in both AspRs and SerRs leads to greater AspR activity while removing the triple serine loop region results in almost complete loss of AspR activity
evolution
the enzyme belongs to the fold-type II group of pyridoxal 5'-phosphate enzymes
evolution
the enzyme from Zea mays belongs to the type II PLP-dependent enzymes and differs from the enzyme of a vancomycin-resistant bacterium
evolution
Roseobacter litoralis ATCC 49566 / DSM 6996 / JCM 21268 / NBRC 15278 / OCh 149
-
the enzyme belongs to the fold-type II group of pyridoxal 5'-phosphate enzymes
-
malfunction
-
increased levels of enzyme-mediated D-serine production are associated with amyotrophic lateral sclerosis and Alzheimer's disease
malfunction
-
serine racemase is associated with schizophrenia susceptibility in a mouse model, abnormal N-methyl-D-aspartate receptor function is implicated in the pathophysiology of schizophrenia
malfunction
-
serine racemase is associated with schizophrenia susceptibility in humans, abnormal N-methyl-D-aspartate receptor function is implicated in the pathophysiology of schizophrenia
malfunction
-
enzyme knockout mice show increased expression of involucrin and keratin 10 in the epidermis compared to wild-type mice
malfunction
-
enzyme KO mutant mice show reduced D-serine contents, reduced N-methyl-D-aspartate receptor activity, and impaired learning and memory abilities, altered morphological features of brain of SR-KO mice, altered behaviur and neurodegeneration in KO mice, phenotypes of three SR-KO mouse strains, overview. Enzyme expression in the liver is upregulated in nSR-KO_ITC mice
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
malfunction
-
repeated administration of methamphetamine results in behavioral sensitization in wild-type, but not in knockout mutant Srr-KO mice, while METH-induced acute hyperlocomotion is similar in wild-type and mutant mice. Pretreatment with D-serine does not affect the development of behavioral sensitization after repeated methamphetamine administration
malfunction
-
serine racemase is implicated with NMDA receptor dysfunction and schizophrenia
malfunction
D-Asp levels are significantly lower in the hippocampi and frontal cortices of SRR-knockout mice, approximately half the levels recorded from wild-type mice. These results are consistent with those from a previous study. In contrast, D-Asp abundance is not altered in the cerebellums or testes of SRR-knockout mice
malfunction
HEK-293T cells expressing the wild-type enzyme and hyperactive mutant Q155D show resistance to staurosporine-induced apoptosis, compared with nontransfected HEK-293T cells and cells expressing the catalytically-dead enzyme mutant K56G. The wild-type enzyme-expressing cells also show a significant higher viability than the cells expressing hyperactive mutant Q155D enzyme mutant. Elevated phosphorylation levels of Bcl-2 at Ser70 and Akt at Ser473 and Thr308, which are related to cell survival, occur in the cells expressing wild-type enzyme and mutant Q155D, elevated levels of acetyl CoA and ATP in cells expressing the wild-type enzyme. Phenotypes, overview
malfunction
no significant decreases in the intracellular D-Asp levels are observed in the SRR-KO cells, the intracellular concentration of D-Ser in the SRR-KO PC12 cells is visibly lower than that in the controls
malfunction
-
serine racemase is associated with schizophrenia susceptibility in a mouse model, abnormal N-methyl-D-aspartate receptor function is implicated in the pathophysiology of schizophrenia
-
malfunction
-
enzyme KO mutant mice show reduced D-serine contents, reduced N-methyl-D-aspartate receptor activity, and impaired learning and memory abilities, altered morphological features of brain of SR-KO mice, altered behaviur and neurodegeneration in KO mice, phenotypes of three SR-KO mouse strains, overview. Enzyme expression in the liver is upregulated in nSR-KO_ITC mice
-
malfunction
-
enzyme knockout mice show increased expression of involucrin and keratin 10 in the epidermis compared to wild-type mice
-
physiological function
-
inhibition of D-serine synthesis caused by translocation of the enzyme to the membrane provides a fail-safe mechanism to prevent NMDA receptor overactivation in vicinal cells or synapses
physiological function
-
the enzyme is responsible for D-serine production in the central nervous system, where D-serine acts as a co-agonist of the N-methyl-D-aspartate receptor ion channels
physiological function
-
the enzyme is responsible for the biosynthesis of the neurotransmitter D-serine, which activates N-methyl-D-aspartate receptors in the central nervous system
physiological function
-
serine racemase catalyses the synthesis of the transmitter/neuromodulator D-serine, which plays a major role in synaptic plasticity and N-methyl D-aspartate receptor neurotoxicity
physiological function
-
D-serine is an endogenous coagonist of the N-methyl-D-aspartate-type glutamate receptor in the central nervous system and its synthesis is catalyzed by serine racemase
physiological function
-
D-serine, synthesized by the enzyme, is an important coagonist at the NR1 subunit of the NMDA receptor class of glutamate receptors
physiological function
-
role of D-serine as an endogenous agonist of N-methyl-D-aspartate receptors (NMDARs). D-Serine is required for NMDAR activity during normal neurotransmission as well as NMDAR overactivation that takes place in neurodegenerative conditions
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
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
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
physiological function
-
serine racemase is a key player in neuron activity and in neuropathologies. D-serine is the essential co-agonist of the N-methyl-D-aspartate receptor, that mediates neurotransmission, synaptic plasticity, cell migration and long term potentiation. High and low D-serine levels have been associated with distinct neuropathologies, aging-related deficits and psychiatric disorders due to either hyper- or hypo-activation of the receptor. Serine racemase dual activity is regulated by ATP, divalent cations, cysteine nitrosylation, post-translational modifications, and interactions with proteins that bind either at the N- or C-terminus. Molecular basis of catalysis, regulation and conformational plasticity, overview
physiological function
-
serine racemase is an enzyme which synthesizes D-serine, an endogenous co-agonist of N-methyl-D-aspartate (NMDA) receptors. N-methyl-D-aspartate receptors play a role in behavioral abnormalities observed after administration of the psychostimulant, methamphetamine. Role of serine racemase in behavioral sensitization in mice after repeated administration of methamphetamine, overview
physiological function
-
through cross-talk between allosteric and active sites, intracellular ATP and glycine control D-serine homeostasis, and, indirectly, NMDA receptor activity. The N-methyl D-aspartate (NMDA) receptors play a key role in excitatory neurotransmission, and control learning, memory and synaptic plasticity. Their activity is modulated by the agonist glutamate and by the co-agonists D-serine and glycine
physiological function
free D-serine (D-Ser) plays a crucial role in regulating brain function in mammals. In the brain, D-Ser is synthesized by Ser racemase, the enzyme produces D-Ser from L-Ser in a pyridoxal 5'-phosphate-dependent manner. D-Ser binds to the glycine-binding site of the NMDA receptor and potentiates glutamatergic neurotransmission in the central nervous system. Astroglia and/or neuron-derived D-Ser regulates NMDA receptor-dependent long-term potentiation and/or depression in hypothalamic and hippocampal excitatory synapses. Ser racemase also exhibits dehydratase activity toward several hydroxyamino acids
physiological function
human serine racemase catalyzes both the synthesis and the degradation of D-serine, an obligatory co-agonist of the glutamatergic NMDA receptors. It is allosterically controlled by ATP, which increases its activity around 7fold through a cooperative binding mechanism. Serine racemase is allosterically inhibited by NADH and reduced nicotinamide derivatives suggesting a physiological regulation of hSR activity by the glycolytic flux in neurons. NADH binding counteracts ATP activation of the enzyme with a complete loss of cooperativity
physiological function
-
many endospore-forming bacteria embed alanine racemases into their spore coats, and these enzymes are thought to convert the L-alanine germinant into D-alanine, a spore germination inhibitor. Clostridium difficile spores can respond to a diverse set of amino acid co-germinants and alanine racemase 2, Alr2, EC 5.1.1.1, can accommodate serine as a substrate. L-alanine is a co-germinant, and D-alanine also functions as a co-germinant. L- and D-serine are also co-germinants for Clostridium difficile spores. Only the L-form of alanine can trigger spore germination when added with taurocholic acid. Gene alr2 is dispensable for germination in response to L-alanine but essential for germination in response to D-alanine
physiological function
most of the endogenous free D-serine (about 90%) in the brain is produced by serine racemase. D-Serine in the brain is involved in neurodegenerative disorders and epileptic states as an endogenous co-agonist of the NMDA-type glutamate receptor
physiological function
rat PC-12 cells rely on a non-SRR-based mechanism to produce the majority of its D-Asp
physiological function
serine racemase (SerR) is a pyridoxal 5'-phosphate-dependent enzyme catalyzing the racemization of L-Ser to D-Ser. In mammals, D-Ser is an endogenous coagonist required for the activation of N-methyl-D-aspartate receptors (NMDARs)
physiological function
serine racemase (SerR) is a pyridoxal 5'-phosphate-dependent enzyme catalyzing the racemization of L-Ser to D-Ser. In mammals, D-Ser is an endogenous coagonist required for the activation of N-methyl-D-aspartate receptors (NMDARs)
physiological function
serine racemase catalyzes the production of D-serine, a co-agonist of the N-methyl-D-aspartatereceptor (NMDAR), contribution of the enzyme in the NMDAR-mediated neuronal cell death process. The racemization reaction catalyzed by serine racemase may have a more protective role against apoptosis than the alpha,beta-elimination reaction
physiological function
serine racemase is a key player in apoptosis and necrosis
physiological function
serine racemase is a key player in apoptosis and necrosis, physiological regulation of serine racemase, overview. NMDAR-mediated Ca2+ influx at postsynaptic neurons involves Ca2+/calmodulin-dependent activation of neuronal NO synthase. The NO produced here diffuses into adjacent astrocytes or neurons to nitrosylate and inhibit the serine racemase and activate D-amino acid oxidase (DAAO). Cys113, identified as the target residue of serine racemase nitrosylation, is in close proximity to the ATP-binding region and thus nitrosylation might displace ATP from its binding site and inactivate the enzyme. ATP and NO reciprocally activate and inhibit the enzyme by acting at the same protein site. Synthesis of both neuronal and astrocytic D-serine in the brain is dependent on 3-phosphoglycerate dehydrogenase, an enzyme that occurs mainly in astrocytes and which catalyzes the first step in L-serine biosynthesis: L-serine shuttles from astrocytes into neurons where it is transformed by neuronal SR to D-serine. Serine racemase D-serine-related pathway in neuronal apoptosis, D-serine and the enzyme are involved in controlling the extent of NMDAR activation and neurotoxic insults observed in many central nervous disorders, like Alzheimer's disease, amylothrophic lateral sclerosis (ALS), and epilepsy, and also stroke and ischemia, detailed overview
physiological function
serine racemase is a pyridoxal 5'-phosphate dependent enzyme responsible for the synthesis of D-serine, a neuromodulator of the NMDA receptors. Its activity is modulated by several ligands, including ATP, divalent cations and protein interactors. The enzyme is negatively regulated by reversible S-nitrosylation of cysteine residues, C113, C128, and C269, overview
physiological function
serine racemase, SRR, is involved in D-aspartate biosynthesis, SRR is responsible for D-Asp production in certain organs and/or tissues
physiological function
the enzyme is responsible for D-serine biosynthesis in vivo
physiological function
the mammalian Ser racemase homologue encoded by T01H8.2 from Caenorhabditis elegans exhibits racemase activity, it also shows dehydratase activity toward several hydroxyamino acids. The enzyme is not critical for Ser metabolism in vico. T01H8.2 Ser, Asp, and Ala racemase activities are one to two orders of magnitude lower than those of human Ser racemase. Other than the T01H8.2 gene, there is no known gene within the Caenorhabditis elegans genome that is orthologous to a Ser racemase gene, therefore, D-Ser may be biosynthesized by an enzyme(s) that does not belong to the Ser racemase family, or an enzyme that has not yet been classified as a member of this family.T01H8.2 exhibit higher dehydratase activity toward L-THA in vitro, T01H8.2 might play a role in the metabolism of this amino acid in vivo. T01H8.2-mediated dehydration of diet-derived L-THA may be necessary to avoid toxicity
physiological function
-
many endospore-forming bacteria embed alanine racemases into their spore coats, and these enzymes are thought to convert the L-alanine germinant into D-alanine, a spore germination inhibitor. Clostridium difficile spores can respond to a diverse set of amino acid co-germinants and alanine racemase 2, Alr2, EC 5.1.1.1, can accommodate serine as a substrate. L-alanine is a co-germinant, and D-alanine also functions as a co-germinant. L- and D-serine are also co-germinants for Clostridium difficile spores. Only the L-form of alanine can trigger spore germination when added with taurocholic acid. Gene alr2 is dispensable for germination in response to L-alanine but essential for germination in response to D-alanine
-
physiological function
-
role of D-serine as an endogenous agonist of N-methyl-D-aspartate receptors (NMDARs). D-Serine is required for NMDAR activity during normal neurotransmission as well as NMDAR overactivation that takes place in neurodegenerative conditions
-
physiological function
-
D-serine is an endogenous coagonist of the N-methyl-D-aspartate-type glutamate receptor in the central nervous system and its synthesis is catalyzed by serine racemase
-
physiological function
-
the mammalian Ser racemase homologue encoded by T01H8.2 from Caenorhabditis elegans exhibits racemase activity, it also shows dehydratase activity toward several hydroxyamino acids. The enzyme is not critical for Ser metabolism in vico. T01H8.2 Ser, Asp, and Ala racemase activities are one to two orders of magnitude lower than those of human Ser racemase. Other than the T01H8.2 gene, there is no known gene within the Caenorhabditis elegans genome that is orthologous to a Ser racemase gene, therefore, D-Ser may be biosynthesized by an enzyme(s) that does not belong to the Ser racemase family, or an enzyme that has not yet been classified as a member of this family.T01H8.2 exhibit higher dehydratase activity toward L-THA in vitro, T01H8.2 might play a role in the metabolism of this amino acid in vivo. T01H8.2-mediated dehydration of diet-derived L-THA may be necessary to avoid toxicity
-
additional information
a A65S hSDH mutant of serine dehydratase, EC 4.2.1.13, acquires an additional function of using D-serine as a substrate
additional information
-
a A65S hSDH mutant of serine dehydratase, EC 4.2.1.13, acquires an additional function of using D-serine as a substrate
additional information
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circular dichroism spectral analysis of wild-type and mutant enzymes, overview
additional information
-
rat serine racemase lacks the C-terminal PDZrecognition sequence
additional information
-
roles of quaternary structure and cysteine residues in the activity of human serine racemase, structure-function relationships of the recombinant enzyme, overview
additional information
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Alr2 racemase is the sixth most highly expressed gene during Clostridium difficile spore formation
additional information
enzyme activity site structure, docking and modeling, overview
additional information
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enzyme activity site structure, docking and modeling, overview
additional information
enzyme activity site structure, docking and modeling, overview
additional information
homology modeling of the ligand-free form of the human enzyme, in which the X-ray crystal structure of ligand-free rat enzyme, PDB ID 3HMK, is used as a template
additional information
role of individual residues at position 150-152, overview
additional information
-
role of individual residues at position 150-152, overview
additional information
role of individual residues at position 150-152, overview
additional information
role of individual residues at position 150-152, overview
additional information
-
role of individual residues at position 150-152, overview
additional information
structural comparison with Rattus norvegicus and Schizosaccharomyces pombe serine racemases reveals a similar arrangement of active-site residues but a different orientation of the C-terminal helix, structure modeling, overview. Active site structure comparisons
additional information
-
structural comparison with Rattus norvegicus and Schizosaccharomyces pombe serine racemases reveals a similar arrangement of active-site residues but a different orientation of the C-terminal helix, structure modeling, overview. Active site structure comparisons
additional information
-
Alr2 racemase is the sixth most highly expressed gene during Clostridium difficile spore formation
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P150S/P151S/F152S
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site-directed mutagenesis, the mutant shows altered substrate specificity and activity compared to the wild-type enzyme
P151S/F152S
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site-directed mutagenesis, the mutant shows altered substrate specificity and activity compared to the wild-type enzyme
P150S/P151S/Y152S
site-directed mutagenesis, the mutant shows altered substrate specificity and activity compared to the wild-type enzyme
D213A
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site-directed mutagenesis, the mutation abolishes the enzyme activation by Mg2+ and Na+
E207A
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site-directed mutagenesis, the mutation abolishes the enzyme activation by Mg2+ and Na+
H84A
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site-directed mutagenesis, the mutant shows reduced racemase and dehydrase activities compared to the wild-type enzyme
K111A
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site-directed mutagenesis, the mutant shows reduced racemase and dehydrase activities compared to the wild-type enzyme
K56A
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site-directed mutagenesis, catalytically inactive mutant
P150S
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site-directed mutagenesis, the mutant shows reduced racemase and dehydrase activities compared to the wild-type enzyme
R132A
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site-directed mutagenesis, the mutant shows reduced racemase and dehydrase activities compared to the wild-type enzyme
S80A
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site-directed mutagenesis, catalytically inactive mutant
S80C
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site-directed mutagenesis, the mutant shows reduced racemase and dehydrase activities compared to the wild-type enzyme
S81A
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site-directed mutagenesis, Ser81 is located on the opposite side of K56, the mutation converts the enzyme from serine racemase to L-serine dehydrase, the mutant shows no racemase activity and has significantly reduced D-serine dehydrase activity, but it completely retains its L-serine dehydrase activity
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
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
H152S
-
ratio of elimination reaction to racemization is 1.4 compared to 3.7 in wild-type
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
N154F
-
ratio of elimination reaction to racemization is 0.33 compared to 3.7 in wild-type
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
P153S
-
ratio of elimination reaction to racemization is 0.24 compared to 3.7 in wild-type
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
E219A/D225A
-
neither the serine racemase nor the dehydratase activities of the E219A/D225A serine racemase mutant are affected by the addition of Mg2+. The kcat/Km values of the mutant decrease to 16% (for L-Ser) and 23% (for D-Ser) of those of the wild type protein in the racemase reaction and to 36% (for L-Ser) and 26% (for D-Ser) in the dehydratase reaction
H150S/P151S/F152S
site-directed mutagenesis, the mutant shows altered substrate specificity and activity compared to the wild-type enzyme
C2D/C6D
-
site-directed mutagenesis
S82A
site-directed mutagenesis
K39A
-
site-directed mutagenesis, kinetically inactive mutant, the mutation disrupts the binding of the co-factor that is essential for catalysis (pyridoxal 5'-phosphate), the mutant shows altered binding kinetics with L-alanine and D-alanine, weak binding to L- and D-serine
K39A
-
site-directed mutagenesis, kinetically inactive mutant, the mutation disrupts the binding of the co-factor that is essential for catalysis (pyridoxal 5'-phosphate), the mutant shows altered binding kinetics with L-alanine and D-alanine, weak binding to L- and D-serine
-
K56G
-
inactive
K56G
site-directed mutagenesis, catalytically inactive mutant
Q155D
-
ratio of elimination reaction to racemization is 0.25 compared to 3.7 in wild-type
Q155D
site-directed mutagenesis, catalytically hyperactive mutant, the mutant shows enhanced racemization and reduced alpha,beta-elimination activities
additional information
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introducing the triple serine loop region into SerRs promotes aspartate racemization
additional information
T01H8.2 deletion allele (tm1988)
additional information
-
T01H8.2 deletion allele (tm1988)
additional information
-
T01H8.2 deletion allele (tm1988)
-
additional information
introducing the triple serine loop region into SerRs promotes aspartate racemization
additional information
-
circular dichroism spectral analysis of wild-type and mutant enzymes, overview
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
additional information
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in neonatal mice with knock-out of protein interacting with C-kinase, PICK1 the levels of D-serine are selectively decreased in the forebrain
additional information
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serine racemase knock-out mice show a 90% decrease in forebrain D-serine content and a reduced neurotoxicity induced by NMDA- and beta-amyloid1-42-peptide injections in the forebrain
additional information
-
targeted disruption of serine racemase results in profoundly altered glutamatergic neurotransmission and subtle but significant behavioral abnormailites that reflect hyperactivity and impaired spatial memory, and that are consistent with elevated anxiety
additional information
-
enzyme mutants that cannot bind phosphatidylinositol(4,5)-bisphosphate lose their membrane localizations and display a 4fold enhancement of catalytic activity. Moreover, metabotropic glutamate receptors activation of the enzyme activity is abolished by inhibiting phospholipase C
additional information
-
generation of mice with an ENU-induced mutation, SrrY269stop, that results in a complete loss of Srr activity and dramatically reduced D-serine levels. Mutant mice display behaviors relevant to schizophrenia, including impairments in prepulse inhibition, sociability and spatial discrimination. Behavioral deficits are exacerbated by an NMDAR antagonist and ameliorated by D-serine or the atypical antipsychotic clozapine. Expression profiling reveals that the Srr mutation influences several genes that are linked to schizophrenia and cognitive ability, expression pattern of the enzyme in mutant brain tissues, detailed phenotype, overview
additional information
-
targeted deletion of the enzyme lead to markedly diminished nitric oxide formation and neurotoxicity in the brain, NO formation and nitrosylation of NO targets are reduced. Knockout mice show highly diminished infarct volume following middle cerebral artery occlusion in several regions of the brains, while the number and sensitivity of the NMDA receptors are increased, phenotype, overview
additional information
-
generation of enzyme knockout mutant mice, phenotypes, overview
additional information
introducing the triple serine loop region into SerRs promotes aspartate racemization
additional information
-
introducing the triple serine loop region into SerRs promotes aspartate racemization
additional information
-
generation of enzyme knockout mutant mice, phenotypes, overview
-
additional information
-
generation of mice with an ENU-induced mutation, SrrY269stop, that results in a complete loss of Srr activity and dramatically reduced D-serine levels. Mutant mice display behaviors relevant to schizophrenia, including impairments in prepulse inhibition, sociability and spatial discrimination. Behavioral deficits are exacerbated by an NMDAR antagonist and ameliorated by D-serine or the atypical antipsychotic clozapine. Expression profiling reveals that the Srr mutation influences several genes that are linked to schizophrenia and cognitive ability, expression pattern of the enzyme in mutant brain tissues, detailed phenotype, overview
-
additional information
introducing the triple serine loop region into SerRs promotes aspartate racemization
additional information
SRR overexpression increases D-serine and pyruvate and decreases D-serine uptake and alanine-serine-cysteine transporter ASCT2 mRNA but does not affect D-amino acid oxidase. SRR knockdown does not alter any of the parameters
additional information
induction of mutation by CRISPR/Cas9 genome editing in Srr loci in PC-12 cells. Generation of SRR-KO PC-12 cells. Two independent SRR-KO PC12 cell clones, Nos. 16 and 21, are identified/selected as SRR-KO samples. Clone No. 16 contains a 1-bp insertion in exon 4 of both alleles, resulting in a frame-shift and premature termination of SRR translation to yield a severely truncated protein (69 amino acid residues). The No. 21 clone possesses an 8-bp and 1-bp deletion in each locus of SRR exon 4, and results in a frame-shift and truncation of the enzyme of the protein size by 66 amino acid residues. Both truncated proteins are predicted to lose the enzyme activity. No significant decreases in the intracellular D-Asp levels are observed in the SRR-KO cells
additional information
construction of a modified enzyme, which has a unique lysino-D-alanyl residue at the active site, and also exhibits catalytic activities. The substrate serine is actually trapped in the active site of the modified enzyme, suggesting that the lysino-D-alanyl residue acts as a catalytic base in the same manner as inherent Lys57 of the wild-type enzyme
additional information
-
construction of a modified enzyme, which has a unique lysino-D-alanyl residue at the active site, and also exhibits catalytic activities. The substrate serine is actually trapped in the active site of the modified enzyme, suggesting that the lysino-D-alanyl residue acts as a catalytic base in the same manner as inherent Lys57 of the wild-type enzyme
additional information
the yeast enzyme is covalently modified with dehydroalanine derived from its natural substrate serine, giving a serine racemase with catalytically active lysinoalanyl residue. The modification is not reversed by incubation in 20 mM potassium phosphate buffer, pH 7.2, without serine for several days at room temperature. The enzyme remains partially active even though its essential Lys57 inherently forming a Schiff base with the coenzyme pyridoxal 5'-phosphate is converted to N(6)-(R-2-amino-2-carboxyethyl)-L-lysyl (lysino-D-alanyl) residue. The alpha-amino group of the D-alanyl moiety of the lysino-D-alanyl residue serves as a catalytic base in the same manner asthe epsilon-amino group of Lys57 of the original enzyme. The specific activities of modified spSR for L-serine racemization and L-serine dehydration are 54%, and 68%, respectively, of those of the original spSR
additional information
-
the yeast enzyme is covalently modified with dehydroalanine derived from its natural substrate serine, giving a serine racemase with catalytically active lysinoalanyl residue. The modification is not reversed by incubation in 20 mM potassium phosphate buffer, pH 7.2, without serine for several days at room temperature. The enzyme remains partially active even though its essential Lys57 inherently forming a Schiff base with the coenzyme pyridoxal 5'-phosphate is converted to N(6)-(R-2-amino-2-carboxyethyl)-L-lysyl (lysino-D-alanyl) residue. The alpha-amino group of the D-alanyl moiety of the lysino-D-alanyl residue serves as a catalytic base in the same manner asthe epsilon-amino group of Lys57 of the original enzyme. The specific activities of modified spSR for L-serine racemization and L-serine dehydration are 54%, and 68%, respectively, of those of the original spSR
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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
brenda
Svensson, M.L.; Gatenbeck, S.
The presence of two serine racemases in Streptomyces garyphalus, a D-cycloserine producer
Arch. Microbiol.
129
213-215
1981
Streptomyces garyphalus
-
brenda
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 (Q9QZX7), Mus musculus
brenda
Wu, S.; Barger, S.W.; Sims, T.J.
Schwann cell and epineural fibroblast expression of serine racemase
Brain Res.
1020
161-166
2004
Rattus norvegicus
brenda
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
brenda
Dunlop, D.S.; Neidle, A.
Regulation of serine racemase activity by amino acids
Brain Res. Mol. Brain Res.
133
208-214
2005
Mus musculus
brenda
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 (Q9QZX7), Mus musculus
brenda
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
brenda
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
brenda
Foltyn, V.N.; Bendikov, I.; De Miranda, J.; Panizzutti, R.; Dumin, E.; Shleper, M.; Li, P.; Toney, M.D.; Kartvelishvily, E.; Wolosker, H.
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Mus musculus
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Wu, S.Z.; Bodles, A.M.; Porter, M.M.; Griffin, W.S.; Basile, A.S.; Barger, S.W.
Induction of serine racemase expression and D-serine release from microglia by amyloid beta-peptide
J. Neuroinflammation
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2004
Rattus norvegicus
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Arias, C.A.; Martin-Martinez, M.; Blundell, T.L.; Arthur, M.; Courvalin, P.; Reynolds, P.E.
Characterization and modelling of VanT: a novel, membrane-bound, serine racemase from vancomycin-resistant Enterococcus gallinarum BM4174
Mol. Microbiol.
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1999
Enterococcus gallinarum, Enterococcus gallinarum BM4174
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Neidle, A.; Dunlop, D.S.
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Mus musculus
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Shoji, K.; Mariotto, S.; Ciampa, A.R.; Suzuki, H.
Regulation of serine racemase activity by D-serine and nitric oxide in human glioblastoma cells
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2006
Homo sapiens
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Dememes, D.; Mothet, J.P.; Nicolas, M.T.
Cellular distribution of d-serine, serine racemase and d-amino acid oxidase in the rat vestibular sensory epithelia
Neuroscience
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2006
Rattus norvegicus
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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
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2003
Ambystoma tigrinum, Mus musculus, Rattus norvegicus
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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
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2005
Mus musculus
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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
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1999
Mus musculus (Q9QZX7)
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Wolosker, H.; Sheth, K.N.; Takahashi, M.; Mothet, J.P.; Brady, R.O., Jr.; Ferris, C.D.; Snyder, S.H.
Purification of serine racemase: biosynthesis of the neuromodulator D-serine
Proc. Natl. Acad. Sci. USA
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1999
Rattus norvegicus
brenda
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
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2002
Mus musculus
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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.
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2005
Homo sapiens
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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.
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2007
Rattus norvegicus, Homo sapiens (Q9GZT4)
brenda
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.
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2007
Homo sapiens
brenda
Takeyama, K.; Yoshikawa, M.; Oka, T.; Kawaguchi, M.; Suzuki, T.; Hashimoto, A.
Ketamine enhances the expression of serine racemase and D-amino acid oxidase mRNAs in rat brain
Eur. J. Pharmacol.
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2006
Rattus norvegicus
brenda
Hashimoto, A.; Yoshikawa, M.; Andoh, H.; Yano, H.; Matsumoto, H.; Kawaguchi, M.; Oka, T.; Kobayashi, H.
Effects of MK-801 on the expression of serine racemase and D-amino acid oxidase mRNAs and on the D-serine levels in rat brain
Eur. J. Pharmacol.
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2007
Rattus norvegicus
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Dun, Y.; Mysona, B.; Itagaki, S.; Martin-Studdard, A.; Ganapathy, V.; Smith, S.B.
Functional and molecular analysis of D-serine transport in retinal Mueller cells
Exp. Eye Res.
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2007
Rattus norvegicus (Q76EQ0)
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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.
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2007
Mus musculus
brenda
Ohnishi, M.; Saito, M.; Wakabayashi, S.; Ishizuka, M.; Nishimura, K.; Nagata, Y.; Kasai, S.
Purification and characterization of serine racemase from a hyperthermophylum Pyrobaculum islandicum
J. Bacteriol.
190
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2007
Pyrobaculum islandicum, Pyrobaculum islandicum (Q2V0H1)
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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
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2007
Mus musculus, Mus musculus C57/BL6J
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Steffek, A.E.; Haroutunian, V.; Meador-Woodruff, J.H.
Serine racemase protein expression in cortex and hippocampus in schizophrenia
NeuroReport
17
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2006
Homo sapiens
brenda
Fujitani, Y.; Nakajima, N.; Ishihara, K.; Oikawa, T.; Ito, K.; Sugimoto, M.
Molecular and biochemical characterization of a serine racemase from Arabidopsis thaliana
Phytochemistry
67
668-674
2006
Arabidopsis thaliana (Q2PGG3), Arabidopsis thaliana
brenda
Fujitani, Y.; Horiuchi, T.; Ito, K.; Sugimoto, M.
Serine racemases from barley, Hordeum vulgare L., and other plant species represent a distinct eukaryotic group: gene cloning and recombinant protein characterization
Phytochemistry
68
1530-1536
2007
Hordeum vulgare (A5HUN0), Hordeum vulgare
brenda
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)
brenda
Yoshikawa, M.; Shinomiya, T.; Takayasu, N.; Tsukamoto, H.; Kawaguchi, M.; Kobayashi, H.; Oka, T.; Hashimoto, A.
Long-term treatment with morphine increases the D-serine content in the rat brain by regulating the mRNA and protein expressions of serine racemase and D-amino acid oxidase
J. Pharmacol. Sci.
107
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2008
Rattus norvegicus (Q76EQ0)
brenda
Sugimoto, M.; Sakamoto, W.; Fujitani, Y.
Localization and expression of serine racemase in Arabidopsis thaliana
Amino Acids
36
587-590
2009
Arabidopsis thaliana
brenda
Takayasu, N.; Yoshikawa, M.; Watanabe, M.; Tsukamoto, H.; Suzuki, T.; Kobayashi, H.; Noda, S.
The serine racemase mRNA is expressed in both neurons and glial cells of the rat retina
Arch. Histol. Cytol.
71
123-129
2008
Rattus norvegicus (Q76EQ0)
brenda
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
brenda
Takarada, T.; Hinoi, E.; Takahata, Y.; Yoneda, Y.
Serine racemase suppresses chondrogenic differentiation in cartilage in a Sox9-dependent manner
J. Cell. Physiol.
215
320-328
2008
Rattus norvegicus
brenda
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.
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2008
Mus musculus
brenda
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
brenda
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
brenda
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
brenda
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
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brenda
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
brenda
Yamauchi, T.; Goto, M.; Wu, H.Y.; Uo, T.; Yoshimura, T.; Mihara, H.; Kurihara, T.; Miyahara, I.; Hirotsu, K.; Esaki, N.
Serine racemase with catalytically active lysinoalanyl residue
J. Biochem.
145
421-424
2009
Schizosaccharomyces pombe (O59791), Schizosaccharomyces pombe
brenda
Goto, M.; Yamauchi, T.; Kamiya, N.; Miyahara, I.; Yoshimura, T.; Mihara, H.; Kurihara, T.; Hirotsu, K.; Esaki, N.
Crystal structure of a homolog of mammalian serine racemase from Schizosaccharomyces pombe
J. Biol. Chem.
284
25944-25952
2009
Schizosaccharomyces pombe (O59791), Schizosaccharomyces pombe
brenda
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
brenda
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
brenda
Sikka, P.; Walker, R.; Cockayne, R.; Wood, M.J.; Harrison, P.J.; Burnet, P.W.
D-Serine metabolism in C6 glioma cells: Involvement of alanine-serine-cysteine transporter (ASCT2) and serine racemase (SRR) but not D-amino acid oxidase (DAO)
J. Neurosci. Res.
88
1829-1840
2010
Rattus norvegicus (Q76EQ0)
brenda
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
brenda
Gogami, Y.; Ito, K.; Kamitani, Y.; Matsushima, Y.; Oikawa, T.
Occurrence of D-serine in rice and characterization of rice serine racemase
Phytochemistry
70
380-387
2009
Oryza sativa (Q7XSN8), Oryza sativa
brenda
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
brenda
Balan, L.; Foltyn, V.N.; Zehl, M.; Dumin, E.; Dikopoltsev, E.; Knoh, D.; Ohno, Y.; Kihara, A.; Jensen, O.N.; Radzishevsky, I.S.; Wolosker, H.
Feedback inactivation of D-serine synthesis by NMDA receptor-elicited translocation of serine racemase to the membrane
Proc. Natl. Acad. Sci. USA
106
7589-7594
2009
Rattus norvegicus
brenda
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
brenda
Wolosker, H.
Serine racemase and the serine shuttle between neurons and astrocytes
Biochim. Biophys. Acta
1814
1558-1566
2011
Mus musculus
brenda
Gogami, Y.; Kobayashi, A.; Ikeuchi, T.; Oikawa, T.
Site-directed mutagenesis of rice serine racemase: evidence that Glu219 and Asp225 mediate the effects of Mg2+ on the activity
Chem. Biodivers.
7
1579-1590
2010
Oryza sativa
brenda
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
brenda
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
brenda
Ito, T.; Murase, H.; Maekawa, M.; Goto, M.; Hayashi, S.; Saito, H.; Maki, M.; Hemmi, H.; Yoshimura, T.
Metal ion dependency of serine racemase from Dictyostelium discoideum
Amino Acids
43
1567-1576
2012
Dictyostelium discoideum
brenda
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
brenda
Ito, T.; Maekawa, M.; Hayashi, S.; Goto, M.; Hemmi, H.; Yoshimura, T.
Catalytic mechanism of serine racemase from Dictyostelium discoideum
Amino Acids
44
1073-1084
2013
Dictyostelium discoideum
brenda
Harty, M.; Nagar, M.; Atkinson, L.; Legay, C.M.; Derksen, D.J.; Bearne, S.L.
Inhibition of serine and proline racemases by substrate-product analogues
Bioorg. Med. Chem. Lett.
24
390-393
2014
Schizosaccharomyces pombe
brenda
Wang, W.; Barger, S.W.
Roles of quaternary structure and cysteine residues in the activity of human serine racemase
BMC Biochem.
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63
2011
Homo sapiens
brenda
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
brenda
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.
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2013
Homo sapiens
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Campanini, B.; Spyrakis, F.; Peracchi, A.; Mozzarelli, A.
Serine racemase: a key player in neuron activity and in neuropathologies
Front. Biosci.
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2013
Homo sapiens
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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
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2011
Homo sapiens, Mus musculus, Rattus norvegicus
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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
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2014
Mus musculus, Mus musculus C57BL/6
brenda
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
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2012
Mus musculus
brenda
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
brenda
Zou, L.; Song, Y.; Wang, C.; Sun, J.; Wang, L.; Cheng, B.; Fan, J.
Crystal structure of maize serine racemase with pyridoxal 5-phosphate
Acta Crystallogr. Sect. F
72
165-171
2016
Zea mays (F5CAQ9), Zea mays
brenda
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, Penaeus monodon (A0A0U4MRI4), Crassostrea gigas (A0A0U5AKI6), Mus musculus (Q9QZX7), Mus musculus
brenda
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
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2016
Homo sapiens (Q9GZT4), Homo sapiens
brenda
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
brenda
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)
brenda
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
brenda
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)
brenda
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
brenda
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
brenda
Canu, N.; Ciotti, M.T.; Pollegioni, L.
Serine racemase a key player in apoptosis and necrosis
Front. Synaptic Neurosci.
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9
2014
Homo sapiens (Q9GZT4), Mus musculus (Q9QZX7)
brenda
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)
brenda
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
Rattus norvegicus (Q76EQ0), Mus musculus (Q9QZX7)
brenda
Shrestha, R.; Lockless, S.W.; Sorg, J.A.
A Clostridium difficile alanine racemase affects spore germination and accommodates serine as a substrate
J. Biol. Chem.
292
10735-10742
2017
Clostridioides difficile, Clostridioides difficile UK1
brenda
Kubota, T.; Shimamura, S.; Kobayashi, T.; Nunoura, T.; Deguchi, S.
Distribution of eukaryotic serine racemases in the bacterial domain and characterization of a representative protein in Roseobacter litoralis Och 149
Microbiology
162
53-61
2016
Roseobacter litoralis (F7ZG00), Roseobacter litoralis ATCC 49566 / DSM 6996 / JCM 21268 / NBRC 15278 / OCh 149 (F7ZG00)
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