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Information on EC 5.1.1.18 - serine racemase and Organism(s) Oryza sativa and UniProt Accession Q7XSN8
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5.1.1.18 serine racemaseIUBMB Comments
A pyridoxal-phosphate protein that is highly selective for L-serine as substrate. D-Serine is found in type-II astrocytes in mammalian brain, where it appears to be an endogenous ligand of the glycine site of N-methyl-D-aspartate (NMDA) receptors [1,2]. The reaction can also occur in the reverse direction but does so more slowly at physiological serine concentrations .
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Word Map
- 5.1.1.18
- d-serine
- n-methyl-d-aspartate
-
co-agonist
-
nmdars
- astrocyte
-
d-amino
-
schizophrenia
-
neurotransmission
- pyridoxal
-
hypofunction
- d-aspartate
-
glutamatergic
-
5'-phosphate-dependent
-
nmda-type
- d-ser
-
plp-dependent
-
nmdar-mediated
- pharmacology
- medicine
-
alanine-serine-cysteine
- drug development
-
glycine-binding
-
n-methyl-d
-
vante
-
brain-enriched
-
gliotransmitter
-
nmdar-dependent
The taxonomic range for the selected organisms is: Oryza sativa
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
serine racemase, srace, t01h8.2, ser racemase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-, -
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
77114-08-0
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mg2+ increases the catalytic efficiency of the serine racemase activity of SerR and decreases that of the serine dehydratase activity. The structure of SerR is distorted by the addition of Mg2+, which is probably involved in the enzyme regulation
Mg2+
-
required for serine racemase activity, Glu219 and Asp225 are the essential amino acid residues for Mg2+ to affect both kinds of enzyme activities (racemase and dehydratase)
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ATP
ATP decreases the serine racemase activity of SerR but increases the serine dehydratase activity
additional information
SerR was inhibited by pyridoxal 5'-phosphate-enzyme inhibitors
-
additional information
-
SerR was inhibited by pyridoxal 5'-phosphate-enzyme inhibitors
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2 - 3
D-serine
-
wild type enzyme, in the absence of Mg2+, pH and temperature not specified in the publication
8.9
D-serine
-
wild type enzyme, in the presence of 1 mM Mg2+, pH and temperature not specified in the publication
40
D-serine
-
mutant enzyme E219A/D225A, in the absence of Mg2+, pH and temperature not specified in the publication
48
D-serine
-
mutant enzyme E219A/D225A, in the presence of 1 mM Mg2+, pH and temperature not specified in the publication
10
L-serine
-
wild type enzyme, in the presence of 1 mM Mg2+, pH and temperature not specified in the publication
18
L-serine
-
wild type enzyme, in the absence of Mg2+, pH and temperature not specified in the publication
78
L-serine
-
mutant enzyme E219A/D225A, in the presence of 1 mM Mg2+, pH and temperature not specified in the publication
130
L-serine
-
mutant enzyme E219A/D225A, in the absence of Mg2+, pH and temperature not specified in the publication
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.12
D-serine
-
mutant enzyme E219A/D225A, in the absence of Mg2+, pH and temperature not specified in the publication
0.14
D-serine
-
mutant enzyme E219A/D225A, in the presence of 1 mM Mg2+, pH and temperature not specified in the publication
0.2
D-serine
-
wild type enzyme, in the presence of 1 mM Mg2+, pH and temperature not specified in the publication
0.31
D-serine
-
wild type enzyme, in the absence of Mg2+, pH and temperature not specified in the publication
0.26
L-serine
-
mutant enzyme E219A/D225A, in the presence of 1 mM Mg2+, pH and temperature not specified in the publication
0.31
L-serine
-
wild type enzyme, in the presence of 1 mM Mg2+, pH and temperature not specified in the publication
0.36
L-serine
-
wild type enzyme, in the absence of Mg2+, pH and temperature not specified in the publication
0.42
L-serine
-
mutant enzyme E219A/D225A, in the absence of Mg2+, pH and temperature not specified in the publication
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.003
D-serine
-
mutant enzyme E219A/D225A, in the absence of Mg2+, pH and temperature not specified in the publication
0.003
D-serine
-
mutant enzyme E219A/D225A, in the presence of 1 mM Mg2+, pH and temperature not specified in the publication
0.013
D-serine
-
wild type enzyme, in the absence of Mg2+, pH and temperature not specified in the publication
0.022
D-serine
-
wild type enzyme, in the presence of 1 mM Mg2+, pH and temperature not specified in the publication
0.0032
L-serine
-
mutant enzyme E219A/D225A, in the absence of Mg2+, pH and temperature not specified in the publication
0.0033
L-serine
-
mutant enzyme E219A/D225A, in the presence of 1 mM Mg2+, pH and temperature not specified in the publication
0.02
L-serine
-
wild type enzyme, in the absence of Mg2+, pH and temperature not specified in the publication
0.031
L-serine
-
wild type enzyme, in the presence of 1 mM Mg2+, pH and temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
recombinant His-tagged SerR 16.9fold from Escherichia coli strain BL21 (DE3) to homogeneity ny nickel affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
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