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EC Tree
IUBMB Comments 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+.
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
D-3-hydroxyaspartate aldolase, d-HAA,
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D-3-hydroxyaspartate aldolase
D-3-hydroxyaspartate aldolase
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D-3-hydroxyaspartate aldolase
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D-erythro-3-hydroxyaspartate = glycine + glyoxylate
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threo-3-hydroxy-D-aspartate = glycine + glyoxylate
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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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2-amino-3-hydroxybutanedioic acid
aminoacetic acid + oxoacetic acid
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D-3-3,4-dihydroxyphenylserine
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D-erythro-3-3,4-methylenedioxyphenylserine
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D-erythro-3-hydroxyaspartate
glycine + glyoxylate
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
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D-threo-3-3,4-methylenedioxyphenylserine
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D-threo-3-phenylserine
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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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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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EDTA
82% inhibition at 1 mM
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0.4
D-erythro-3-hydroxyaspartate
in 0.02 mM HEPES buffer, pH 8.0, at 30°C
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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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strain IFO 13301
UniProt
brenda
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41633
2 * 41633, calculated from amino acid sequence
43000
2 * 43000, SDS-PAGE
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homodimer
2 * 43000, SDS-PAGE
homodimer
2 * 41633, calculated from amino acid sequence
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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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45
the enzyme retains 50% activity upon heating at 45°C for 30 min
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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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expressed in Escherichia coli XL1-Blue MRFâ cells
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Liu, J.Q.; Dairi, T.; Itoh, N.; Kataoka, M.; Shimizu, S.
A novel enzyme, D-3-hydroxyaspartate aldolase from Paracoccus denitrificans IFO 13301: purification, characterization, and gene cloning
Appl. Microbiol. Biotechnol.
62
53-60
2003
Paracoccus denitrificans (Q8GRC8)
brenda
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4.1.3.41 3-hydroxy-D-aspartate aldolase
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