Information on EC 5.1.1.18 - serine racemase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea

EC NUMBER
COMMENTARY hide
5.1.1.18
-
RECOMMENDED NAME
GeneOntology No.
serine racemase
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-serine = D-serine
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
elimination
-
-
racemization
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
D-serine metabolism
-
-
Glycine, serine and threonine metabolism
-
-
Metabolic pathways
-
-
vancomycin resistance II
-
-
serine metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
serine racemase
A pyridoxal-phosphate protein that is highly selective for L-serine as substrate. D-Serine is found in type-II astrocytes in mammalian brain, where it appears to be an endogenous ligand of the glycine site of N-methyl-D-aspartate (NMDA) receptors [1,2]. The reaction can also occur in the reverse direction but does so more slowly at physiological serine concentrations [4].
CAS REGISTRY NUMBER
COMMENTARY hide
77114-08-0
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
salamander
-
-
Manually annotated by BRENDA team
strain BM4174, vancomycin-resistant
-
-
Manually annotated by BRENDA team
strain BM4174, vancomycin-resistant
-
-
Manually annotated by BRENDA team
cv. Haruna nijo
SwissProt
Manually annotated by BRENDA team
C57BL/6J mice
-
-
Manually annotated by BRENDA team
strain C57BL/6JJcl and DBA/2JJcl
-
-
Manually annotated by BRENDA team
isozymes I and II
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
-
the eukaryotic serine racemase from Dictyostelium discoideum is a fold-type II pyridoxal 5'-phosphate-dependent enzyme
malfunction
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
beta-chloro-L-alanine
pyruvate + NH3 + ?
show the reaction diagram
-
the artificial serine racemase substrate is degraded via alpha,beta-elimination
-
-
?
D-alanine
L-alanine
show the reaction diagram
-
-
-
-
r
D-serine
L-serine
show the reaction diagram
D-serine
pyruvate + H2O
show the reaction diagram
-
alpha,beta-elimination reaction
-
-
?
D-serine
pyruvate + NH3
show the reaction diagram
D-serine
S-serine
show the reaction diagram
-
-
-
-
?
D-threonine
L-threonine
show the reaction diagram
13% of the activity with L-serine
-
-
r
L-alanine
D-alanine
show the reaction diagram
L-arginine
D-arginine
show the reaction diagram
7% of the activity with L-serine
-
-
?
L-glutamine
D-glutamine
show the reaction diagram
4.5% of the activity with L-serine
-
-
?
L-serine
D-serine
show the reaction diagram
L-serine
pyruvate + NH3
show the reaction diagram
L-serine O-sulfate
O-sulfopyruvate + NH3
show the reaction diagram
L-serine O-sulfate
pyruvate + NH3 + ?
show the reaction diagram
-
the artificial serine racemase substrate is degraded via alpha,beta-elimination
-
-
?
L-serine-O-sulfate
O-sulfopyruvate + NH3
show the reaction diagram
-
elimination reaction
-
-
?
L-threo-3-hydroxyaspartate
pyruvate + NH3 + ?
show the reaction diagram
-
the artificial serine racemase substrate is degraded via alpha,beta-elimination
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
-
alpha,beta-elimination reaction
-
-
?
L-threonine
?
show the reaction diagram
-
-
-
-
?
L-threonine
D-threonine
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-serine
D-serine
show the reaction diagram
L-threonine
D-threonine
show the reaction diagram
Q2V0H1
-
-
-
r
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ATP
-
Mg-ATP is a stimulatory cofactor
pyridoxal 5'-phosphate
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cu2+
30-40% stimulation
EDTA
-
complete inhibition, provokes a profound conformational change
Fe2+
activates 1.4fold at 1 mM
Na+
-
activates two- to ninefold racemization and dehydration, half-maximal activation concentration is 2.2 mM, Mg2+ and Na+ share the common metal ion-binding site
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Acetohydroxamic acid
-
i.e. Lithostat
adipodihydroxamic acid
-
-
alpha-(hydroxymethyl)-L-serine
-
substrate-product analogue, a modest, linear mixed-type inhibitor of serine racemase
amino-oxyacetic acid
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
Co2+
-
-
cystamine
D-cycloserine
-
2 mM, 64% inhibition
D-Cysteine
-
2 mM, 72% residual activity
Dihydroxyfumarate
-
-
DL-Serine hydroxamate
-
-
DL-Threonine hydroxamate
-
-
glutarodihydroxamic acid
-
-
glycine
Glycine hydroxamate
-
-
hydroxylamine
L-2,3-diaminopropionic acid
-
2 mM, 68% residual activity
L-asparagine
L-aspartic acid
L-aspartic acid beta-hydroxamate
-
a competitive and selective serine racemase inhibitor
L-Cycloserine
-
10 mM, 45% inhibition
L-cysteine
L-cysteine-S-sulfate
-
-
L-erythro-3-hydroxyaspartate
L-homocysteic acid
-
2 mM, 59% residual activity
L-serine-O-sulfate
Maleate
-
-
malonate
malonodihydroxamic acid
-
-
meso-tartrate
-
-
nitric oxide
oxaloacetic acid
-
2 mM, 56% residual activity
oxalodihydroxamic acid
-
-
phenazine
-
non-selective inhibitor
phosphatidylinositol-4,5-bisphosphate
Sodium borohydride
complete inhibition at 1 mM
suberodihydroxamic acid
-
-
succinodihydroxamic acid
-
-
vorinostat
-
i.e. Zolinza
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,4-dithiothreitol
-
chemical reduction with DTT increases the enzyme activity by elevating Vmax
D-serine
-
up to 5fold increase in activity
glutamate receptor interacting protein
-
glycine
-
glycine stabilizes a protein conformation that binds ATP non-cooperatively and with high affinity, the active-site ligand increases the serine racemase affinity for ATP by about 22fold, abolishing cooperativity. ATP increases the noncooperative glycine binding 15fold
metabotropic glutamate receptor
-
i.e. mGluR5, on glia, activation mechanism of the D-serine synthesis needed for NMDA neurotransmission, overview
-
morphine
-
chronic administration significantly augments both serine racemase mRNA and protein expression in all brain regions and leads to slight but significant elevation in the concentration of D-serine in the cortex, striatum, and hippocampus
protein interacting with C kinase 1
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2 - 95.4
D-serine
111
L-alanine
-
-
1 - 185
L-serine
0.49
L-serine O-sulfate
-
pH 8.0, 37°C, presence of 1 mM ATP, elimination reaction
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.004 - 14.5
D-serine
0.02 - 14.8
L-serine
0.49
L-serine O-sulfate
Mus musculus
-
pH 8.0, 37°C, presence of 1 mM ATP, elimination reaction
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.003 - 0.022
D-serine
481
0.001 - 0.031
L-serine
95
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
167
alpha-(hydroxymethyl)-L-serine
-
pH and temperature not specified in the publication
0.69
Dihydroxyfumarate
-
pH 8.0, 37°C
0.366 - 1.64
glycine
1.13
L-asparagine
-
pH 8.0, 37°C
1.9
L-aspartic acid
1.3
L-aspartic acid beta-hydroxamate
-
pH 8.0
0.64
L-cysteine-S-sulfate
-
pH 8.0, 37°C
0.011 - 0.043
L-erythro-3-hydroxyaspartate
0.55
Maleate
-
pH 8.0, 37°C
0.033 - 0.071
malonate
0.66
meso-tartrate
-
pH 8.0, 37°C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.013
phosphatidylinositol-4,5-bisphosphate
Mus musculus
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.083
-
pH 8.0, 37°C
0.13
purified recombinant enzyme
0.139
-
purified His-tagged wild-type enzyme, pH 8.0, 37°C, substrate D-serine
0.263
-
purified His-tagged wild-type enzyme, pH 8.0, 37°C, substrate L-serine
13.6
pH 8.2, 95°C
additional information
-
D-serine concentration in brain areas, overview
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
-
10% of maximum activity
7.7
-
assay at
8 - 9.5
-
-
8
-
assay at
8.1
-
assay at
8.2
; racemase activity
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5
-
negligible activity below
8 - 9.5
high activity within this range
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
95
; both racemase and dehydratase activity
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
of adult cerebellum, weak but significant expression
Manually annotated by BRENDA team
-
mRNA is ubiquitously expressed in all cell layers of proliferating to hypertrophic chondrocytes
Manually annotated by BRENDA team
-
vestibular sensory epithelium, in transitional cells therein, which are parasensory cells located between the sensory epithelium and the dark cells, and in dark cells
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
cell line U87, inverse regulation of enzyme activty by D-serine and nitric oxide
Manually annotated by BRENDA team
-
a microglial cell line
Manually annotated by BRENDA team
-
peripheral expression in cardiac myocyte
Manually annotated by BRENDA team
-
peripheral expression in convoluted tubules
Manually annotated by BRENDA team
-
developing leaf
Manually annotated by BRENDA team
-
Schwann cell and other endoneural components of spinal nerve, lysates of sciatic nerve
Manually annotated by BRENDA team
-
neuronal like cell line
Manually annotated by BRENDA team
-
head of optic nerve
Manually annotated by BRENDA team
-
a retinal Mueller cell line, enzyme expression analysis, uptake of D-serine in Mueller cells is specific for neutral amino acids and excludes anionic and cationic amino acids, specificity and activity of transporters, overview
Manually annotated by BRENDA team
-
tip regions of primary and lateral root
Manually annotated by BRENDA team
-
shoot meristem
Manually annotated by BRENDA team
-
an astrocytoma cell line
Manually annotated by BRENDA team
-
of neonatal rat, mRNA is ubiquitously expressed in all cell layers of proliferating to hypertrophic chondrocytes
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
high amount of the enzyme
Manually annotated by BRENDA team
-
high amount of the enzyme
Manually annotated by BRENDA team
additional information
-
enzyme translocation to the membrane is blocked by a palmitoylation inhibitor, indicating that membrane binding is mediated by fatty acid acylation of the enzyme
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
29000
-
x * 29000, truncated mutant enzyme, SDS-PAGE
35700
x * 35700, about, sequence calculation, x * 36000, recombinant enzyme, SDS-PAGE
36000
x * 35700, about, sequence calculation, x * 36000, recombinant enzyme, SDS-PAGE
36121
-
x * 36121, MALDI-MS, x * 36123, calculated
36123
-
x * 36121, MALDI-MS, x * 36123, calculated
36300
-
x * 36300, calculated, x * 38000, SDS-PAGE
37500
-
2 * 37500, SDS-PAGE, dimer-tetramer equilibrium; 4 * 37500, SDS-PAGE, dimer-tetramer equilibrium
39000
-
2 * 39000, SDS-PAGE
40000
-
2 * 40000, recombinant His-tagged enzyme, SDS-PAGE, the major oligomeric form of recombinant enzyme in aqueous solution. The enzyme is most active as a noncovalent dimer containing one or more free sulfhydryls in the enzymes active center or a modulatory site
44000
3 * 44000, SDS-PAGE; 4 * 44000, native enzyme, SDS-PAGE
55000
-
isoforms A and B, gel filtration
60000
recombinant enzyme, gel filtration
73000
-
x * 93000, isozyme I, x * 73000, isozyme II, SDS-PAGE
74400
-
recombinant His-tagged enzyme, gel filtration
78000
-
gel filtration
80200
-
gel filtration
82900
-
gel filtration
87000
recombinant enzyme, gel filtration
87500
-
recombinant His-tagged enzyme, gel filtration
93000
-
x * 93000, isozyme I, x * 73000, isozyme II, SDS-PAGE
130000
gel filtration
137000
native enzyme, gel filtration
143000
native enzyme, light scattering-refraction
153000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
-
2 * 39000, SDS-PAGE
tetramer
trimer
3 * 44000, SDS-PAGE
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nitrosylation
phospholipoprotein
-
the enzyme is acylated in transfected neuroblastoma cells through the formation of an oxyester bond with serine or threonine residues using palmitate or octanoic acid as precursors. Phosphorylation of Thr227 is also required for steady-state binding of the enzyme to the membrane under basal, nonstimulated condition. No S-palmitoylation of the enzyme in SH-SY5Y neuroblastoma cells, but O-palmitoylation
phosphoprotein
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified recombinant mutant C2D/C6D by sitting drop vapor diffusion, 10 mg/ml protein in 20 mM Tris-HCl, pH 8.0, 100 mM NaCl, 10% glycerol, 0.05 mM PLP, 2 mM MgCl2, 5 mM dithiothreitol, mixed with 25% PEG 3350, 200 mM sodium malonate, and 50 mM MnCl2 as the reservoir solution, 4 days, the selenomethionine-labeled enzyme crystals grow under similar conditions, X-ray diffraction structure determination and analysis at 1.5-1.7 A resolution
-
purified recombinant mutant C2D/C6D by sitting drop vapor diffusion, 35 mg/ml protein, from 55% v/v Tacsimate, i.e. 1.8305 M malonic acid, 0.25 M ammonium citrate tribasic, 0.12 M succinic acid, 0.3 M DL-malic acid, 0.4 M sodium acetate trihydrate, 0.5 M sodium formate, and 0.16 M ammonium tartrate dibasic, pH 8.0, and 100 mM Bis-Tris propane, pH 7.8, 10 days, X-ray diffraction structure determination and analysis at 1.8-1.95 A resolution
-
free wild-type enzyme, wild-type enzyme in complex with the ATP analogue AMP-PCP, and the modified enzyme in complex with serine, vapor diffusion method at 20°C, 0.003 ml of protein solution with 2.2 mg/ml protein and 10 mM Tris-HCl buffer, pH 8.0, are mixed with an equal volume of reservoir solution containing 28% w/v PEG 4000, 200 mM sodium acetate, and 100 mM Tris-HCl, pH 8.5, and equilibrated against 450 ml of the reservoir solution, for the ligand complexed enzyme, 10 mM AMP-PCP and 0.2 M MgCl2 are added, X-ray diffraction structure determination and analysis at at 1.7 A, 1.9 A, and 2.2 A resolution, respectively
-
native and modified enzyme, X-ray diffraction structure determination and analysis at 1.7 A resolution
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 10.5
-
purified recombinant enzyme, stable at
726663
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
8 h, purified enzyme, 100 mM Tris-HCl buffer, pH 7.8, containing 0.01 mM pyridoxal 5’-phosphate, 95.2% remaining activity
75
8 h, purified enzyme, 100 mM Tris-HCl buffer, pH 7.8, containing 0.01 mM pyridoxal 5’-phosphate, 67.1% remaining activity
95
8 h, purified enzyme, 100 mM Tris-HCl buffer, pH 7.8, containing 0.01 mM pyridoxal 5’-phosphate, 29.8% remaining activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, stable for at least 4 days
-
enzyme residues C217 and K221 are important for Mg2+ binding and enzyme stability
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, purified recombinant enzyme, 20 mM sodium phosphate buffer, pH 8.0, 5 days, no loss of activity, but in 20 mM sodium or potassium phosphate buffer, pH 7.0, the enzyme is unstable and becomes inactivated, forming aggregates, leading to loss of about 30% of the initial activity after storage for 3 days
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
both isoforms A and B
-
expression in Escherichia coli with N-terminal His-tag, purification protocol from inclusion bodies
-
native enzyme by anion exchange chromatography, recombinant enzyme from Escherichia coli by treatment with L-arginine and anion exchange chromatography
Ni-NTA agarose column chromatography
-
purification of isozyme I, partial purification of isozyme II
-
recombinant C-terminally His6-tagged wild-type and mutant enzymes from Escherichia coli strain MC1061 by nickel affinity chromatography and gel filtration
-
recombinant enzyme
-
recombinant enzyme expressed in insect cells
-
recombinant enzyme from Escherichia coli strain MC1061 by hydrophobic interaction and anion exchange chromatography, followed by ATP affinity chromatography and dialysis
-
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant His-tagged enzyme from Escherichia coli strain BL21-CodonPlus(DE3)-RIL by metal affinity chromatography
-
recombinant His-tagged enzyme mutant from Escherichia coli strain Rosetta 2 (DE3) by affinity chromatography and gel filtration to over 98% purity
recombinant His-tagged SerR 16.9fold from Escherichia coli strain BL21 (DE3) to homogeneity ny nickel affinity chromatography
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain Rosetta II (DE3) by nickel affinity chromatography
-
recombinant His6-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) using Talon resin chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cloning from genomic DNA, DNA and amino acid sequence determination
-
DNA and amino acid sequence determination and analysis, expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
DNA and amino acid sequence determination and analysis, phylogenetic analysis, expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
enzyme expression in Escherichia coli strain MC1061
-
enzyme expression of His-tagged enzyme in Escherichia coli strain BL21-CodonPlus(DE3)-RIL
-
expressed in Escherichia coli BL21(DE3) cells
-
expression of C-terminally His6-tagged wild-type and mutant enzymes in Escherichia coli strain MC1061
-
expression of GST-tagged fusion protein containing amino acid residue 150-190 of the mouse enzyme, expression of His-tagged enzyme in Cavia porcellus and Oryctolagus cuniculus, quantitative real-time PCR enzyme expression analysis
-
expression of His-tagged enzyme mutant in Escherichia coli strain Rosetta 2 (DE3)
expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain Rosetta II (DE3)
-
expression of His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
-
expression of the highly active His-tagged serine racemase from brain in moderate halophilic bacteria, the recombinant enzyme shows 2.6fold higher elimination than racemization activity
-
expression of untagged and of N-terminally His6-tagged and C-terminally FLAG-tagged enzyme in COS-7 cells, co-expression with glutamate receptor interacting protein or FLAG-tagged glutamate receptor interacting protein domain PDZ6
-
expression oof wild-type and mutant enzyme in Escherichia coli strain Rosetta 2 (DE3)
-
gene serR, encoding the enzyme, is located on chromosome 4 of the genomic DNA, phylogenetic analysis, cloning and expression of the His-tagged enzyme in Escherichia coli strain BL21 (DE3)
gene srr, DNA and amino acid sequence determination and anaylsis, expression in Escherichia coli
HEK293 cells transfected with wild-type enzyme and metabotropic glutamate receptor display a 4fold increase in enzyme activity upon treatment with the metabotropic glutamate receptor agonist dihydroxyphenylglycine
-
optimization for expression in Escherichia coli
-
overexpression in ATDC5 cell and in COS7 cell
-
overexpression of HA-tagged enzyme in SH-SY5Y neuroblastoma cells and in HEK293 cells, coexpression with palmitic acid leads to acylation of the enzyme
-
quantitative expression analysis
-
total RNA is isolated from rMC-1 cells reverse-transcribed into cDNA and subjected to PCR using rat-specific SR primers, expression analysis of the enzyme in retinal Mueller cells
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
L-serine or D-serine, but not D-proline, increase the expression of SRR in C6 cells when added to the cell culture medium
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D213A
-
site-directed mutagenesis, the mutation abolishes the enzyme activation by Mg2+ and Na+
E207A
-
site-directed mutagenesis, the mutation abolishes the enzyme activation by Mg2+ and Na+
H84A
-
site-directed mutagenesis, the mutant shows reduced racemase and dehydrase activities compared to the wild-type enzyme
K111A
-
site-directed mutagenesis, the mutant shows reduced racemase and dehydrase activities compared to the wild-type enzyme
K56A
-
site-directed mutagenesis, catalytically inactive mutant
P150S
-
site-directed mutagenesis, the mutant shows reduced racemase and dehydrase activities compared to the wild-type enzyme
R132A
-
site-directed mutagenesis, the mutant shows reduced racemase and dehydrase activities compared to the wild-type enzyme
S80A
-
site-directed mutagenesis, catalytically inactive mutant
S80C
-
site-directed mutagenesis, the mutant shows reduced racemase and dehydrase activities compared to the wild-type enzyme
S81A
-
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
C2D/C6D
-
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
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
N154F
-
ratio of elimination reaction to racemization is 0.33 compared to 3.7 in wild-type
P153S
-
ratio of elimination reaction to racemization is 0.24 compared to 3.7 in wild-type
Q155D
-
ratio of elimination reaction to racemization is 0.25 compared to 3.7 in wild-type
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
C2D/C6D
-
site-directed mutagenesis
S82A
-
site-directed mutagenesis
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
medicine
pharmacology
-
because D-serine affects NMDAR signaling throughout the brain, serine racemase is a promising target for the treatment of disorders related to NMDAR dysfunction