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Literature summary extracted from
- Characterization of a homologue of mammalian serine racemase from Caenorhabditis elegans the enzyme is not critical for the metabolism of serine invivo (2016), Genes Cells, 21, 966-977 .
Activating Compound
| EC Number | Activating Compound | Comment | Organism | Structure |
|---|---|---|---|---|
| 5.1.1.18 | ATP | activates | Homo sapiens |  |
| 5.1.1.18 | ATP | activates | Caenorhabditis elegans | |
| 5.1.1.18 | additional information | EDTA has no significant effect on enzyme activity | Homo sapiens | |
| 5.1.1.18 | additional information | EDTA has no significant effect on enzyme activity | Caenorhabditis elegans |
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 5.1.1.18 | gene T01H8.2, DNA and amino acid sequence determination and analysis, recombinant expression of C-terminally His-tagged enzyme in Escherichia coli. Other than the T01H8.2 gene, there is no known gene within the Caenorhabditis elegans genome that is orthologous to a Ser racemase gene | Caenorhabditis elegans |
| 5.1.1.18 | recombinant expression of N-terminally His-tagged enzyme in Escherichia coli | Homo sapiens |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 5.1.1.18 | additional information | T01H8.2 deletion allele (tm1988) | Caenorhabditis elegans |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 5.1.1.18 | additional information | EDTA has no significant effect on enzyme activity. No inhibition by D-threo-3-hydroxyaspartate | Caenorhabditis elegans | |
| 5.1.1.18 | additional information | EDTA has no significant effect on enzyme activity. No inhibition by D-threo-3-hydroxyaspartate | Homo sapiens |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 5.1.1.18 | 6.12 | - |
L-serine | recombinant enzyme, pH 8.0, 30°C | Caenorhabditis elegans | |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 5.1.1.18 | Mg2+ | activates | Homo sapiens | |
| 5.1.1.18 | Mg2+ | activates | Caenorhabditis elegans | |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 5.1.1.18 | L-serine | Homo sapiens | - |
D-serine | - |
r | |
| 5.1.1.18 | additional information | Caenorhabditis elegans | the enzyme does not appear to metabolize D- and L-Ser in vivo | ? | - |
? | |
| 5.1.1.18 | additional information | Caenorhabditis elegans N2 | the enzyme does not appear to metabolize D- and L-Ser in vivo | ? | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 5.1.1.18 | Caenorhabditis elegans | Q93968 | - |
- |
| 5.1.1.18 | Caenorhabditis elegans N2 | Q93968 | - |
- |
| 5.1.1.18 | Homo sapiens | Q9GZT4 | - |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 5.1.1.18 | recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography and dialysis, to near homogeneity | Caenorhabditis elegans |
| 5.1.1.18 | recombinant His-tagged enzyme from Escherichia coli nickel affinity chromatography and dialysis, to near homogeneity | Homo sapiens |
Source Tissue
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|---|
| 5.1.1.18 | astrocyte | - |
Homo sapiens | - |
| 5.1.1.18 | forebrain | - |
Homo sapiens | - |
| 5.1.1.18 | neuron | - |
Homo sapiens | - |
Specific Activity [micromol/min/mg]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 5.1.1.18 | additional information | - |
comparison of racemase activity of recombinant T01H8.2 and human Ser racemase toward several L-amino acids | Homo sapiens |
| 5.1.1.18 | additional information | - |
comparison of racemase activity of recombinant T01H8.2 and human Ser racemase toward several L-amino acids | Caenorhabditis elegans |
| 5.1.1.18 | 0.00146 | - |
purified recombinant enzyme, L-Ser racemase activity, pH 8.0, 30°C | Caenorhabditis elegans |
| 5.1.1.18 | 0.148 | - |
purified recombinant enzyme, L-Ser racemase activity, pH 8.0, 30°C | Homo sapiens |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 5.1.1.18 | L-alanine | very low activity | Homo sapiens | D-alanine | - |
r | |
| 5.1.1.18 | L-alanine | very low activity | Caenorhabditis elegans | D-alanine | - |
r | |
| 5.1.1.18 | L-alanine | very low activity | Caenorhabditis elegans N2 | D-alanine | - |
r | |
| 5.1.1.18 | L-aspartate | low activity | Homo sapiens | D-aspartate | - |
r | |
| 5.1.1.18 | L-aspartate | low activity | Caenorhabditis elegans | D-aspartate | - |
r | |
| 5.1.1.18 | L-aspartate | low activity | Caenorhabditis elegans N2 | D-aspartate | - |
r | |
| 5.1.1.18 | L-serine | - |
Homo sapiens | D-serine | - |
r | |
| 5.1.1.18 | L-serine | - |
Caenorhabditis elegans | D-serine | - |
r | |
| 5.1.1.18 | L-serine | - |
Caenorhabditis elegans N2 | D-serine | - |
r | |
| 5.1.1.18 | L-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 | Caenorhabditis elegans | D-threo-3-hydroxyaspartate | - |
r | |
| 5.1.1.18 | L-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 | Homo sapiens | D-threo-3-hydroxyaspartate | - |
r | |
| 5.1.1.18 | additional information | the enzyme does not appear to metabolize D- and L-Ser in vivo | Caenorhabditis elegans | ? | - |
? | |
| 5.1.1.18 | 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 | Homo sapiens | ? | - |
? | |
| 5.1.1.18 | 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 | Caenorhabditis elegans | ? | - |
? | |
| 5.1.1.18 | additional information | the enzyme does not appear to metabolize D- and L-Ser in vivo | Caenorhabditis elegans N2 | ? | - |
? | |
| 5.1.1.18 | 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 | Caenorhabditis elegans N2 | ? | - |
? | |
| 5.1.1.18 | rac-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 | Caenorhabditis elegans | D-threo-3-hydroxyaspartate | - |
? | |
| 5.1.1.18 | rac-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 | Homo sapiens | D-threo-3-hydroxyaspartate | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 5.1.1.18 | Ser racemase | - |
Homo sapiens |
| 5.1.1.18 | T01H8.2 | - |
Caenorhabditis elegans |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 5.1.1.18 | 30 | - |
assay at | Caenorhabditis elegans |
Turnover Number [1/s]
| EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 5.1.1.18 | 0.357 | - |
L-serine | recombinant enzyme, pH 8.0, 30°C | Caenorhabditis elegans | |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 5.1.1.18 | 8 | - |
assay at | Caenorhabditis elegans |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 5.1.1.18 | pyridoxal 5'-phosphate | - |
Homo sapiens | |
| 5.1.1.18 | pyridoxal 5'-phosphate | - |
Caenorhabditis elegans | |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 5.1.1.18 | 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 | Homo sapiens |
| 5.1.1.18 | 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 | Caenorhabditis elegans |
kcat/KM [mM/s]
| EC Number | kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 5.1.1.18 | 0.058 | - |
L-serine | recombinant enzyme, pH 8.0, 30°C | Caenorhabditis elegans | |
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