Information on EC 4.3.1.27 - threo-3-hydroxy-D-aspartate ammonia-lyase

for references in articles please use BRENDA:EC4.3.1.27
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The expected taxonomic range for this enzyme is: Delftia

EC NUMBER
COMMENTARY hide
4.3.1.27
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RECOMMENDED NAME
GeneOntology No.
threo-3-hydroxy-D-aspartate ammonia-lyase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
threo-3-hydroxy-D-aspartate = oxaloacetate + NH3
show the reaction diagram
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SYSTEMATIC NAME
IUBMB Comments
threo-3-hydroxy-D-aspartate ammonia-lyase (oxaloacetate-forming)
A pyridoxal-phosphate protein. The enzyme, purified from the bacterium Delftia sp. HT23, also has activity against L-threo-3-hydroxyaspartate, L-erythro-3-hydroxyaspartate, and D-serine. Different from EC 4.3.1.20, erythro-3-hydroxy-L-aspartate ammonia-lyase and EC 4.3.1.16, threo-3-hydroxy-L-aspartate ammonia-lyase. Requires a divalent cation such as Mn2+, Co2+ or Ni2+.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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-
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Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-serine
?
show the reaction diagram
poor substrate
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?
D-threo-3-hydroxyaspartate
oxaloacetate + NH3
show the reaction diagram
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?
L-erythro-3-hydroxyaspartate
?
show the reaction diagram
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-
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?
L-serine
?
show the reaction diagram
poor substrate
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?
L-threo-3-hydroxyaspartate
?
show the reaction diagram
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-
-
?
L-threo-3-hydroxyaspartate
oxaloacetate + NH3
show the reaction diagram
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-
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?
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
activator
Co2+
the recombinant enzyme is highly activated by Co2+
Fe2+
activator
Mn2+
the recombinant enzyme is highly activated by Mn2+
Ni2+
the recombinant enzyme is highly activated by Ni2+
Zn2+
activator
additional information
no activity is detected when Sn2+ or Cu2+ is added
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
EDTA
the enzyme is modestly inhibited by EDTA (27% inhibition at 1 mM)
hydroxylamine
the enzyme is strongly inhibited by hydroxylamine (91.2% inhibition at 1 mM)
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.15
D-serine
at pH 8.5 and 50°C
0.42
D-threo-3-hydroxyaspartate
at pH 8.5 and 50°C
0.16
L-erythro-3-hydroxyaspartate
at pH 8.5 and 50°C
38.7
L-serine
at pH 8.5 and 50°C
6.16
L-threo-3-hydroxyaspartate
at pH 8.5 and 50°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
8.68
D-serine
at pH 8.5 and 50°C
10.93
D-threo-3-hydroxyaspartate
at pH 8.5 and 50°C
8.68
L-erythro-3-hydroxyaspartate
at pH 8.5 and 50°C
0.18
L-serine
at pH 8.5 and 50°C
3.03
L-threo-3-hydroxyaspartate
at pH 8.5 and 50°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5.91
D-serine
at pH 8.5 and 50°C
25.96
D-threo-3-hydroxyaspartate
at pH 8.5 and 50°C
54.25
L-erythro-3-hydroxyaspartate
at pH 8.5 and 50°C
0.0047
L-serine
at pH 8.5 and 50°C
0.49
L-threo-3-hydroxyaspartate
at pH 8.5 and 50°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.18
cell extract, at 50°C, pH 8.5
21.3
after 115.8fold purification, at 50°C, pH 8.5
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PDB
SCOP
CATH
UNIPROT
ORGANISM
Delftia sp. (strain HT23);
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
36000
gel filtration
40300
calculated from amino acid sequence
40900
calculated from the deduced amino acid sequence of the recombinant enzyme
41000
1 * 41000, SDS-PAGE
41600
MALDI-TOF mass spectrometry
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
1 * 41000, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystals of D-THA DH belong to space group I4-1-22, single-wavelength anomalous diffraction data are collected to a resolution of 2.0 A using synchrotron radiation
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, HiPrep Q column chromatography, HiTrap phenyl column chromatography, Superdex-200 gel filtration, Resource Q column chromatography, and HiTrap butyl column chromatography
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli JM109 cells
overexpressed using Rhodococcus erythropolis expression system
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the enzyme is induced by 3-hydroxyaspartate in the medium
the enzyme is not induced by D-serine, D-threonine, D-aspartate, or peptone
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K43A
the mutant enzyme shows no detectable activity