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Literature summary for 4.3.1.27 extracted from
- Purification, characterization and amino acid sequence of a novel enzyme, D-threo-3-hydroxyaspartate dehydratase, from Delftia sp. HT23 (2010), J. Biochem., 148, 705-712.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expressed in Escherichia coli JM109 cells | Delftia sp. HT23 |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| K43A | the mutant enzyme shows no detectable activity | Delftia sp. HT23 |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| EDTA | the enzyme is modestly inhibited by EDTA (27% inhibition at 1 mM) | Delftia sp. HT23 |  |
| hydroxylamine | the enzyme is strongly inhibited by hydroxylamine (91.2% inhibition at 1 mM) | Delftia sp. HT23 | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.15 | - |
D-serine | at pH 8.5 and 50°C | Delftia sp. HT23 | |
| 0.16 | - |
L-erythro-3-hydroxyaspartate | at pH 8.5 and 50°C | Delftia sp. HT23 | |
| 0.42 | - |
D-threo-3-hydroxyaspartate | at pH 8.5 and 50°C | Delftia sp. HT23 | |
| 6.16 | - |
L-threo-3-hydroxyaspartate | at pH 8.5 and 50°C | Delftia sp. HT23 | |
| 38.7 | - |
L-serine | at pH 8.5 and 50°C | Delftia sp. HT23 | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Ca2+ | activator | Delftia sp. HT23 | |
| Co2+ | the recombinant enzyme is highly activated by Co2+ | Delftia sp. HT23 | |
| Fe2+ | activator | Delftia sp. HT23 | |
| Mn2+ | the recombinant enzyme is highly activated by Mn2+ | Delftia sp. HT23 | |
| additional information | no activity is detected when Sn2+ or Cu2+ is added | Delftia sp. HT23 | |
| Ni2+ | the recombinant enzyme is highly activated by Ni2+ | Delftia sp. HT23 | |
| Zn2+ | activator | Delftia sp. HT23 | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 36000 | - |
gel filtration | Delftia sp. HT23 |
| 40300 | - |
calculated from amino acid sequence | Delftia sp. HT23 |
| 40900 | - |
calculated from the deduced amino acid sequence of the recombinant enzyme | Delftia sp. HT23 |
| 41000 | - |
1 * 41000, SDS-PAGE | Delftia sp. HT23 |
| 41600 | - |
MALDI-TOF mass spectrometry | Delftia sp. HT23 |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Delftia sp. HT23 | B2DFG5 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| ammonium sulfate precipitation, HiPrep Q column chromatography, HiTrap phenyl column chromatography, Superdex-200 gel filtration, Resource Q column chromatography, and HiTrap butyl column chromatography | Delftia sp. HT23 |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 0.18 | - |
cell extract, at 50°C, pH 8.5 | Delftia sp. HT23 |
| 21.3 | - |
after 115.8fold purification, at 50°C, pH 8.5 | Delftia sp. HT23 |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| D-serine | poor substrate | Delftia sp. HT23 | ? | - |
? | |
| D-threo-3-hydroxyaspartate | - |
Delftia sp. HT23 | oxaloacetate + NH3 | - |
? | |
| L-erythro-3-hydroxyaspartate | - |
Delftia sp. HT23 | ? | - |
? | |
| L-serine | poor substrate | Delftia sp. HT23 | ? | - |
? | |
| L-threo-3-hydroxyaspartate | - |
Delftia sp. HT23 | oxaloacetate + NH3 | - |
? | |
| L-threo-3-hydroxyaspartate | - |
Delftia sp. HT23 | ? | - |
? | |
| additional information | D-erythro-3-hydroxyaspartate is not a substrate | Delftia sp. HT23 | ? | - |
? | |
| additional information | the purified enzyme shows no alanine racemase activity | Delftia sp. HT23 | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| monomer | 1 * 41000, SDS-PAGE | Delftia sp. HT23 |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| D-THA DH | - |
Delftia sp. HT23 |
| D-threo-3-hydroxyaspartate ammonia-lyase | - |
Delftia sp. HT23 |
| D-threo-3-hydroxyaspartate dehydratase | - |
Delftia sp. HT23 |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 50 | - |
- |
Delftia sp. HT23 |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.18 | - |
L-serine | at pH 8.5 and 50°C | Delftia sp. HT23 | |
| 3.03 | - |
L-threo-3-hydroxyaspartate | at pH 8.5 and 50°C | Delftia sp. HT23 | |
| 8.68 | - |
D-serine | at pH 8.5 and 50°C | Delftia sp. HT23 | |
| 8.68 | - |
L-erythro-3-hydroxyaspartate | at pH 8.5 and 50°C | Delftia sp. HT23 | |
| 10.93 | - |
D-threo-3-hydroxyaspartate | at pH 8.5 and 50°C | Delftia sp. HT23 | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8.5 | - |
- |
Delftia sp. HT23 |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| pyridoxal 5'-phosphate | - |
Delftia sp. HT23 | |
Expression
| Organism | Comment | Expression |
|---|---|---|
| Delftia sp. HT23 | the enzyme is not induced by D-serine, D-threonine, D-aspartate, or peptone | additional information |
| Delftia sp. HT23 | the enzyme is induced by 3-hydroxyaspartate in the medium | up |
kcat/KM [mM/s]
| kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.0047 | - |
L-serine | at pH 8.5 and 50°C | Delftia sp. HT23 | |
| 0.49 | - |
L-threo-3-hydroxyaspartate | at pH 8.5 and 50°C | Delftia sp. HT23 | |
| 5.91 | - |
D-serine | at pH 8.5 and 50°C | Delftia sp. HT23 | |
| 25.96 | - |
D-threo-3-hydroxyaspartate | at pH 8.5 and 50°C | Delftia sp. HT23 | |
| 54.25 | - |
L-erythro-3-hydroxyaspartate | at pH 8.5 and 50°C | Delftia sp. HT23 | |
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