5.1.1.18: serine racemase
This is an abbreviated version!
For detailed information about serine racemase, go to the full flat file.
Word Map on EC 5.1.1.18
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5.1.1.18
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d-serine
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n-methyl-d-aspartate
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co-agonist
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nmdars
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astrocyte
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d-amino
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schizophrenia
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neurotransmission
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pyridoxal
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hypofunction
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d-aspartate
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glutamatergic
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5'-phosphate-dependent
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nmda-type
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d-ser
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plp-dependent
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nmdar-mediated
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pharmacology
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medicine
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alanine-serine-cysteine
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drug development
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glycine-binding
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n-methyl-d
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vante
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brain-enriched
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gliotransmitter
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nmdar-dependent
- 5.1.1.18
- d-serine
- n-methyl-d-aspartate
-
co-agonist
-
nmdars
- astrocyte
-
d-amino
-
schizophrenia
-
neurotransmission
- pyridoxal
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hypofunction
- d-aspartate
-
glutamatergic
-
5'-phosphate-dependent
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nmda-type
- d-ser
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plp-dependent
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nmdar-mediated
- pharmacology
- medicine
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alanine-serine-cysteine
- drug development
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glycine-binding
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n-methyl-d
-
vante
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brain-enriched
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gliotransmitter
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nmdar-dependent
Reaction
Synonyms
hSR, More, RiSR, RLO149_c015450, Ser racemase, SerR, SRace, SRR, T01H8.2, Zm-SR, ZmSR
ECTree
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KM Value
KM Value on EC 5.1.1.18 - serine racemase
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0.49
L-serine O-sulfate
pH 8.0, 37°C, presence of 1 mM ATP, elimination reaction
2 - 3
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wild type enzyme, in the absence of Mg2+, pH and temperature not specified in the publication
8.9
D-serine
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wild type enzyme, in the presence of 1 mM Mg2+, pH and temperature not specified in the publication
12.7
D-serine
pH 8.0, 30°C, recombinant mutant P150S/P151S/Y152S
40
D-serine
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mutant enzyme E219A/D225A, in the absence of Mg2+, pH and temperature not specified in the publication
48
D-serine
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mutant enzyme E219A/D225A, in the presence of 1 mM Mg2+, pH and temperature not specified in the publication
10
L-serine
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wild type enzyme, in the presence of 1 mM Mg2+, pH and temperature not specified in the publication
15.1
L-serine
pH 8.0, 30°C, recombinant mutant P150S/P151S/Y152S
18
L-serine
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wild type enzyme, in the absence of Mg2+, pH and temperature not specified in the publication
78
L-serine
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mutant enzyme E219A/D225A, in the presence of 1 mM Mg2+, pH and temperature not specified in the publication
130
L-serine
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mutant enzyme E219A/D225A, in the absence of Mg2+, pH and temperature not specified in the publication
additional information
additional information
kinetics of wild-type and mutant enzymes
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additional information
additional information
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kinetics of wild-type and mutant enzymes
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additional information
additional information
kinetics of the bifunctional enzyme, overview
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additional information
additional information
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kinetics of the bifunctional enzyme, overview
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additional information
additional information
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the enzyme shows no allosteric properties, it is not affected by either L-isoleucine or L-valine, or most of the metal ions
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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
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additional information
additional information
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enzyme shows no allosteric properties
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additional information
additional information
enzyme shows no allosteric properties
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additional information
additional information
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Michaelis-Menten kinetic analysis
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additional information
additional information
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Michaelis-Menten kinetics, kinetics of serine racemase alpha- and beta-elimination activities, overview
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additional information
additional information
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steady-state kinetics of wild-type and mutant enzymes for serine dehydration activity, EC 4.3.1.17, overview
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additional information
additional information
kinetic parameters of Ser dehydratase activity and Asp racemase activity of wild-type and mutant enzymes
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additional information
additional information
Lineweaver-Burk kinetics
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additional information
additional information
Lineweaver-Burk kinetics
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additional information
additional information
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Lineweaver-Burk kinetics
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