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

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Delftia

EC NUMBER
COMMENTARY hide
4.3.1.27
-
RECOMMENDED NAME
GeneOntology No.
threo-3-hydroxy-D-aspartate ammonia-lyase
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
threo-3-hydroxy-D-aspartate = oxaloacetate + NH3
show the reaction diagram
-
-
-
-
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
-
-
-
Manually annotated by BRENDA team
-
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
-
-
?
D-threo-3-hydroxyaspartate
oxaloacetate + NH3
show the reaction diagram
-
-
-
?
L-erythro-3-hydroxyaspartate
?
show the reaction diagram
-
-
-
?
L-serine
?
show the reaction diagram
poor substrate
-
-
?
L-threo-3-hydroxyaspartate
?
show the reaction diagram
-
-
-
?
L-threo-3-hydroxyaspartate
oxaloacetate + NH3
show the reaction diagram
-
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
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
Delftia sp. HT23
B2DFG5
at pH 8.5 and 50°C
10.93
D-threo-3-hydroxyaspartate
Delftia sp. HT23
B2DFG5
at pH 8.5 and 50°C
8.68
L-erythro-3-hydroxyaspartate
Delftia sp. HT23
B2DFG5
at pH 8.5 and 50°C
0.18
L-serine
Delftia sp. HT23
B2DFG5
at pH 8.5 and 50°C
3.03
L-threo-3-hydroxyaspartate
Delftia sp. HT23
B2DFG5
at pH 8.5 and 50°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5.91
D-serine
Delftia sp. HT23
B2DFG5
at pH 8.5 and 50°C
481
25.96
D-threo-3-hydroxyaspartate
Delftia sp. HT23
B2DFG5
at pH 8.5 and 50°C
41381
54.25
L-erythro-3-hydroxyaspartate
Delftia sp. HT23
B2DFG5
at pH 8.5 and 50°C
5740
0.0047
L-serine
Delftia sp. HT23
B2DFG5
at pH 8.5 and 50°C
95
0.49
L-threo-3-hydroxyaspartate
Delftia sp. HT23
B2DFG5
at pH 8.5 and 50°C
9546
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
ORGANISM
UNIPROT
Delftia sp. (strain HT23)
Delftia sp. (strain HT23)
Delftia sp. (strain HT23)
Delftia sp. (strain HT23)
Delftia sp. (strain HT23)
Delftia sp. (strain HT23)
Delftia sp. (strain HT23)
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
-
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
-
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