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
-
alanine-serine-cysteine
- drug development
-
glycine-binding
-
n-methyl-d
-
vante
-
brain-enriched
-
gliotransmitter
-
nmdar-dependent
Reaction
Synonyms
hSR, More, RiSR, RLO149_c015450, Ser racemase, SerR, SRace, SRR, T01H8.2, Zm-SR, ZmSR
ECTree
5.1.1.18 serine racemaseAdvanced search results
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results (Metals Ions
Metals Ions on EC 5.1.1.18 - serine racemase
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METALS and IONS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Ca2+
Mg2+
Mn2+
Na+
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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
Ca2+
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activates racemase racemization at 1 mM in Tris-HCl buffer, but inhibits racemase and dehydrase activities by 50% at 1 mM in borate-NaOH buffer
Ca2+
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stimulation 5-7fold of the enzyme's elimination and racemization activities
Ca2+
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or Mn2+, required, binding konstant 0.0062 mM. Possible glutamatergic-mediated regulation of enzyme via intracellular calcium concentration
Mg2+
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activates two- to ninefold racemization and dehydration at 1 mM in Tris-HCl buffer, but inhibits racemase and dehydrase activities by 50% at 1 mM in borate-NaOH buffer, half-maximal activation concentration is 0.0012 mM, Mg2+ and Na+ share the common metal ion-binding site
Mg2+
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enzyme residues C217 and K221 are important for Mg2+ binding and enzyme stability
Mg2+
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stimulation 5-7fold of the enzyme's elimination and racemization activities
Mg2+
activates the enzyme independently from ATP, the effect due to divalent ion and ATP is additive
Mg2+
activates the enzyme independently from ATP, the effect due to divalent ion and ATP is additive
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+
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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)
Mg2+
enhances both activities of RiSR, racemization and dehydration
Mn2+
activates 3.0fold at 1 mM, synergy between Mg2+ and ATP on activity
Mn2+
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stimulation 5-7fold of the enzyme's elimination and racemization activities
additional information
the enzyme requires divalent cations, effects of metal ions on the enzyme's dehydration activity, overview
additional information
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the enzyme requires divalent cations, effects of metal ions on the enzyme's dehydration activity, overview
additional information
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the enzyme is unique in its stimulation by monovalent cations such as Na+ in addition to Mg2+ and Ca2+
additional information
Mg2+ or Ca2+ cations interact with similar affinity to a specific site of the enzyme, the formers might represent the physiological ligand since the free Mg2+ concentration in the cells is several orders of magnitude higher than the Ca2+ concentration. The racemase activity is independently stimulated by both Mg2+ and ATP
additional information
the enzyme requires pyridoxal 5'-phosphate and divalent cations such as Ca2+, Mg2+, or Mn2+, but not ATP, effects of metal ions on the enzyme's dehydration activity, overview
additional information
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the enzyme requires pyridoxal 5'-phosphate and divalent cations such as Ca2+, Mg2+, or Mn2+, but not ATP, effects of metal ions on the enzyme's dehydration activity, overview
additional information
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activation of serine racemase by divalent cations has been assumed to be a side-effect associated with ATP binding, activation mechanisms and ligand binding, molecular modelling with the human enzyme, overview
additional information
Mg2+ or Ca2+ cations interact with similar affinity to a specific site of the enzyme, the formers might represent the physiological ligand since the free Mg2+ concentration in the cells is several orders of magnitude higher than the Ca2+ concentration. The racemase activity is independently stimulated by both Mg2+ and ATP
