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Literature summary extracted from

  • Maeda, T.; Takeda, Y.; Murakami, T.; Yokota, A.; Wada, M.
    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.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.3.1.27 expressed in Escherichia coli JM109 cells Delftia sp. HT23

Protein Variants

EC Number Protein Variants Comment Organism
4.3.1.27 K43A the mutant enzyme shows no detectable activity Delftia sp. HT23

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.3.1.27 EDTA the enzyme is modestly inhibited by EDTA (27% inhibition at 1 mM) Delftia sp. HT23
4.3.1.27 hydroxylamine the enzyme is strongly inhibited by hydroxylamine (91.2% inhibition at 1 mM) Delftia sp. HT23

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.3.1.27 0.15
-
 D-serine at pH 8.5 and 50°C Delftia sp. HT23
4.3.1.27 0.16
-
 L-erythro-3-hydroxyaspartate at pH 8.5 and 50°C Delftia sp. HT23
4.3.1.27 0.42
-
 D-threo-3-hydroxyaspartate at pH 8.5 and 50°C Delftia sp. HT23
4.3.1.27 6.16
-
 L-threo-3-hydroxyaspartate at pH 8.5 and 50°C Delftia sp. HT23
4.3.1.27 38.7
-
 L-serine at pH 8.5 and 50°C Delftia sp. HT23

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.3.1.27 Ca2+ activator Delftia sp. HT23
4.3.1.27 Co2+ the recombinant enzyme is highly activated by Co2+ Delftia sp. HT23
4.3.1.27 Fe2+ activator Delftia sp. HT23
4.3.1.27 Mn2+ the recombinant enzyme is highly activated by Mn2+ Delftia sp. HT23
4.3.1.27 additional information no activity is detected when Sn2+ or Cu2+ is added Delftia sp. HT23
4.3.1.27 Ni2+ the recombinant enzyme is highly activated by Ni2+ Delftia sp. HT23
4.3.1.27 Zn2+ activator Delftia sp. HT23

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.3.1.27 36000
-
 gel filtration Delftia sp. HT23
4.3.1.27 40300
-
 calculated from amino acid sequence Delftia sp. HT23
4.3.1.27 40900
-
 calculated from the deduced amino acid sequence of the recombinant enzyme Delftia sp. HT23
4.3.1.27 41000
-
 1 * 41000, SDS-PAGE Delftia sp. HT23
4.3.1.27 41600
-
 MALDI-TOF mass spectrometry Delftia sp. HT23

Organism

EC Number Organism UniProt Comment Textmining
4.3.1.27 Delftia sp. HT23 B2DFG5
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.3.1.27 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]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
4.3.1.27 0.18
-
 cell extract, at 50°C, pH 8.5 Delftia sp. HT23
4.3.1.27 21.3
-
 after 115.8fold purification, at 50°C, pH 8.5 Delftia sp. HT23

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.3.1.27 D-serine poor substrate Delftia sp. HT23 ?
-
 ?
4.3.1.27 D-threo-3-hydroxyaspartate
-
 Delftia sp. HT23 oxaloacetate + NH3
-
 ?
4.3.1.27 L-erythro-3-hydroxyaspartate
-
 Delftia sp. HT23 ?
-
 ?
4.3.1.27 L-serine poor substrate Delftia sp. HT23 ?
-
 ?
4.3.1.27 L-threo-3-hydroxyaspartate
-
 Delftia sp. HT23 oxaloacetate + NH3
-
 ?
4.3.1.27 L-threo-3-hydroxyaspartate
-
 Delftia sp. HT23 ?
-
 ?
4.3.1.27 additional information D-erythro-3-hydroxyaspartate is not a substrate Delftia sp. HT23 ?
-
 ?
4.3.1.27 additional information the purified enzyme shows no alanine racemase activity Delftia sp. HT23 ?
-
 ?

Subunits

EC Number Subunits Comment Organism
4.3.1.27 monomer 1 * 41000, SDS-PAGE Delftia sp. HT23

Synonyms

EC Number Synonyms Comment Organism
4.3.1.27 D-THA DH
-
 Delftia sp. HT23
4.3.1.27 D-threo-3-hydroxyaspartate ammonia-lyase
-
 Delftia sp. HT23
4.3.1.27 D-threo-3-hydroxyaspartate dehydratase
-
 Delftia sp. HT23

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4.3.1.27 50
-
-
 Delftia sp. HT23

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.3.1.27 0.18
-
 L-serine at pH 8.5 and 50°C Delftia sp. HT23
4.3.1.27 3.03
-
 L-threo-3-hydroxyaspartate at pH 8.5 and 50°C Delftia sp. HT23
4.3.1.27 8.68
-
 D-serine at pH 8.5 and 50°C Delftia sp. HT23
4.3.1.27 8.68
-
 L-erythro-3-hydroxyaspartate at pH 8.5 and 50°C Delftia sp. HT23
4.3.1.27 10.93
-
 D-threo-3-hydroxyaspartate at pH 8.5 and 50°C Delftia sp. HT23

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.3.1.27 8.5
-
-
 Delftia sp. HT23

Cofactor

EC Number Cofactor Comment Organism Structure
4.3.1.27 pyridoxal 5'-phosphate
-
 Delftia sp. HT23

Expression

EC Number Organism Comment Expression
4.3.1.27 Delftia sp. HT23 the enzyme is not induced by D-serine, D-threonine, D-aspartate, or peptone additional information
4.3.1.27 Delftia sp. HT23 the enzyme is induced by 3-hydroxyaspartate in the medium up

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
4.3.1.27 0.0047
-
 L-serine at pH 8.5 and 50°C Delftia sp. HT23
4.3.1.27 0.49
-
 L-threo-3-hydroxyaspartate at pH 8.5 and 50°C Delftia sp. HT23
4.3.1.27 5.91
-
 D-serine at pH 8.5 and 50°C Delftia sp. HT23
4.3.1.27 25.96
-
 D-threo-3-hydroxyaspartate at pH 8.5 and 50°C Delftia sp. HT23
4.3.1.27 54.25
-
 L-erythro-3-hydroxyaspartate at pH 8.5 and 50°C Delftia sp. HT23