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

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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+.
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain IFO 13301
UniProt
Manually annotated by BRENDA team
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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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-
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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
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-
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?
D-threo-3-phenylserine
?
show the reaction diagram
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-
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?
additional information
?
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the enzyme shows no activity towards L-erythro-3-hydroxyaspartate, L-threo-3-hydroxyaspartate, L-threonine, L-allo-threonine, L-erythro-3-phenylserine, L-threo-3-phenylserine, L-erythro-3-3,4-methylenedioxyphenylserine, and L-threo-3-3,4-methylenedioxyphenylserine
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COFACTOR
ORGANISM
UNIPROT
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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
K+ and Na+ do not have an effect on the enzymatic activity
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INHIBITORS
ORGANISM
UNIPROT
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LITERATURE
IMAGE
EDTA
82% inhibition at 1 mM
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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 30°C
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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 30°C
0.6
crude extract, in 0.02 mM HEPES buffer, pH 8.0, at 30°C
14.6
after 50fold purification, using D-threo-3-3,4-methylenedioxyphenylserine as substrate, in 0.02 mM HEPES buffer, pH 8.0, at 30°C
17.5
after 50fold purification, using D-erythro-3-3,4-methylenedioxyphenylserine as substrate, in 0.02 mM HEPES buffer, pH 8.0, at 30°C
20
after 50fold purification, using D-threonine as substrate, in 0.02 mM HEPES buffer, pH 8.0, at 30°C
25
after 50fold purification, using D-allo-threonine as substrate, in 0.02 mM HEPES buffer, pH 8.0, at 30°C
30
after 50fold purification, using D-erythro-3-hydroxyaspartate as substrate, in 0.02 mM HEPES buffer, pH 8.0, at 30°C
95
after 50fold purification, using D-threo-3-phenylserine as substrate, in 0.02 mM HEPES buffer, pH 8.0, at 30°C
99
after 50fold purification, using D-erythro-3-phenylserine as substrate, in 0.02 mM HEPES buffer, pH 8.0, at 30°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
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LITERATURE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
41633
2 * 41633, calculated from amino acid sequence
43000
2 * 43000, SDS-PAGE
80000
gel filtration
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
2 * 41633, calculated from amino acid sequence; 2 * 43000, SDS-PAGE
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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 30°C
649407
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45
the enzyme retains 50% activity upon heating at 45°C for 30 min
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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
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli XL1-Blue MRF‘ cells
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LINKS TO OTHER DATABASES (specific for EC-Number 4.1.3.41)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)