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Literature summary for 5.1.1.18 extracted from

  • Katane, M.; Saitoh, Y.; Uchiyama, K.; Nakayama, K.; Saitoh, Y.; Miyamoto, T.; Sekine, M.; Uda, K.; Homma, H.
    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 .
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
ATP activates Homo sapiens
ATP activates Caenorhabditis elegans
additional information EDTA has no significant effect on enzyme activity Homo sapiens
additional information EDTA has no significant effect on enzyme activity Caenorhabditis elegans

Cloned(Commentary)

Cloned (Comment) Organism
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
recombinant expression of N-terminally His-tagged enzyme in Escherichia coli Homo sapiens

Protein Variants

Protein Variants Comment Organism
additional information T01H8.2 deletion allele (tm1988) Caenorhabditis elegans

Inhibitors

Inhibitors Comment Organism Structure
additional information EDTA has no significant effect on enzyme activity. No inhibition by D-threo-3-hydroxyaspartate Caenorhabditis elegans
additional information EDTA has no significant effect on enzyme activity. No inhibition by D-threo-3-hydroxyaspartate Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
6.12
-
L-serine recombinant enzyme, pH 8.0, 30°C Caenorhabditis elegans

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ activates Homo sapiens
Mg2+ activates Caenorhabditis elegans

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-serine Homo sapiens
-
D-serine
-
r
additional information Caenorhabditis elegans the enzyme does not appear to metabolize D- and L-Ser in vivo ?
-
?
additional information Caenorhabditis elegans N2 the enzyme does not appear to metabolize D- and L-Ser in vivo ?
-
?

Organism

Organism UniProt Comment Textmining
Caenorhabditis elegans Q93968
-
-
Caenorhabditis elegans N2 Q93968
-
-
Homo sapiens Q9GZT4
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography and dialysis, to near homogeneity Caenorhabditis elegans
recombinant His-tagged enzyme from Escherichia coli nickel affinity chromatography and dialysis, to near homogeneity Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining
astrocyte
-
Homo sapiens
-
forebrain
-
Homo sapiens
-
neuron
-
Homo sapiens
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
comparison of racemase activity of recombinant T01H8.2 and human Ser racemase toward several L-amino acids Homo sapiens
additional information
-
comparison of racemase activity of recombinant T01H8.2 and human Ser racemase toward several L-amino acids Caenorhabditis elegans
0.00146
-
purified recombinant enzyme, L-Ser racemase activity, pH 8.0, 30°C Caenorhabditis elegans
0.148
-
purified recombinant enzyme, L-Ser racemase activity, pH 8.0, 30°C Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-alanine very low activity Homo sapiens D-alanine
-
r
L-alanine very low activity Caenorhabditis elegans D-alanine
-
r
L-alanine very low activity Caenorhabditis elegans N2 D-alanine
-
r
L-aspartate low activity Homo sapiens D-aspartate
-
r
L-aspartate low activity Caenorhabditis elegans D-aspartate
-
r
L-aspartate low activity Caenorhabditis elegans N2 D-aspartate
-
r
L-serine
-
Homo sapiens D-serine
-
r
L-serine
-
Caenorhabditis elegans D-serine
-
r
L-serine
-
Caenorhabditis elegans N2 D-serine
-
r
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
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
additional information the enzyme does not appear to metabolize D- and L-Ser in vivo Caenorhabditis elegans ?
-
?
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 ?
-
?
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 ?
-
?
additional information the enzyme does not appear to metabolize D- and L-Ser in vivo Caenorhabditis elegans N2 ?
-
?
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 ?
-
?
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
-
?
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

Synonyms Comment Organism
Ser racemase
-
Homo sapiens
T01H8.2
-
Caenorhabditis elegans

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
assay at Caenorhabditis elegans

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.357
-
L-serine recombinant enzyme, pH 8.0, 30°C Caenorhabditis elegans

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
assay at Caenorhabditis elegans

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate
-
Homo sapiens
pyridoxal 5'-phosphate
-
Caenorhabditis elegans

General Information

General Information Comment Organism
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
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]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.058
-
L-serine recombinant enzyme, pH 8.0, 30°C Caenorhabditis elegans