Information on EC 4.1.3.41 - 3-hydroxy-D-aspartate aldolase

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The expected taxonomic range for this enzyme is: Paracoccus denitrificans

EC NUMBER
COMMENTARY hide
4.1.3.41
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RECOMMENDED NAME
GeneOntology No.
3-hydroxy-D-aspartate aldolase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
D-erythro-3-hydroxyaspartate = glycine + glyoxylate
show the reaction diagram
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-
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threo-3-hydroxy-D-aspartate = glycine + glyoxylate
show the reaction diagram
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SYSTEMATIC NAME
IUBMB Comments
3-hydroxy-D-aspartate glyoxylate-lyase (glycine-forming)
A pyridoxal-phosphate protein. The enzyme, purified from the bacterium Paracoccus denitrificans IFO 13301, is strictly D-specific as to the alpha-position of the substrate, but accepts both the threo and erythro forms at the beta-position. The erythro form is a far better substrate (about 100-fold). The enzyme can also accept D-allothreonine, D-threonine, erythro-3-phenyl-D-serine and threo-3-phenyl-D-serine. Different from EC 4.1.3.14, erythro-3-hydroxy-L-aspartate aldolase. Requires a divalent cation, such as Mg2+, Mn2+ or Co2+.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain IFO 13301
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
2-amino-3-hydroxybutanedioic acid
aminoacetic acid + oxoacetic acid
show the reaction diagram
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r
allo-threonine
?
show the reaction diagram
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-
-
?
D-3-3,4-dihydroxyphenylserine
?
show the reaction diagram
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-
-
?
D-erythro-3-3,4-methylenedioxyphenylserine
?
show the reaction diagram
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-
-
?
D-erythro-3-hydroxyaspartate
glycine + glyoxylate
show the reaction diagram
the enzyme is strictly D-specific as to the alpha-position, whereas it does not distinguish between threo and erythro forms at the beta-position
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-
?
D-erythro-3-phenylserine
?
show the reaction diagram
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-
-
?
D-threo-3-3,4-methylenedioxyphenylserine
?
show the reaction diagram
-
-
-
?
D-threo-3-phenylserine
?
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
Co2+
2.0fold increase of specific activity in the presence of 1 mM Co2+
Mg2+
5.4fold increase of specific activity in the presence of 1 mM Mg2+
Mn2+
8.1fold increase of specific activity in the presence of 1 mM Mn2+
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
EDTA
82% inhibition at 1 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.4
D-erythro-3-hydroxyaspartate
in 0.02 mM HEPES buffer, pH 8.0, at 30C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.36
after 50fold purification, using DL-threo-3-hydroxyaspartate as substrate, in 0.02 mM HEPES buffer, pH 8.0, at 30C
0.6
crude extract, in 0.02 mM HEPES buffer, pH 8.0, at 30C
14.6
after 50fold purification, using D-threo-3-3,4-methylenedioxyphenylserine as substrate, in 0.02 mM HEPES buffer, pH 8.0, at 30C
17.5
after 50fold purification, using D-erythro-3-3,4-methylenedioxyphenylserine as substrate, in 0.02 mM HEPES buffer, pH 8.0, at 30C
20
after 50fold purification, using D-threonine as substrate, in 0.02 mM HEPES buffer, pH 8.0, at 30C
25
after 50fold purification, using D-allo-threonine as substrate, in 0.02 mM HEPES buffer, pH 8.0, at 30C
30
after 50fold purification, using D-erythro-3-hydroxyaspartate as substrate, in 0.02 mM HEPES buffer, pH 8.0, at 30C
95
after 50fold purification, using D-threo-3-phenylserine as substrate, in 0.02 mM HEPES buffer, pH 8.0, at 30C
99
after 50fold purification, using D-erythro-3-phenylserine as substrate, in 0.02 mM HEPES buffer, pH 8.0, at 30C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
41633
2 * 41633, calculated from amino acid sequence
43000
2 * 43000, SDS-PAGE
80000
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
2 * 41633, calculated from amino acid sequence; 2 * 43000, SDS-PAGE
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 8.5
the enzyme is stable between pH 6.5 and 8.5 for 30 min at 30C
649407
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45
the enzyme retains 50% activity upon heating at 45C for 30 min
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate fractionation, hydroxyapatite column chromatography, DEAE-Toyopearl column chromatography, phenyl-Toyopearl column chromatography, Superdex 200 gel filtration, and Mono Q column chromatography
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli XL1-Blue MRF cells