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Information on EC 4.3.1.16 - threo-3-hydroxy-L-aspartate ammonia-lyase
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EC Tree
4.3.1.16 threo-3-hydroxy-L-aspartate ammonia-lyaseIUBMB Comments
A pyridoxal-phosphate protein. The enzyme, purified from the bacterium Pseudomonas sp. T62, is highly specific, and does not accept any other stereoisomer of 3-hydroxyaspartate. Different from EC 4.3.1.20, erythro-3-hydroxy-L-aspartate ammonia-lyase and EC 4.3.1.27, threo-3-hydroxy-D-aspartate ammonia-lyase. Requires a divalent cation such as Mn2+, Mg2+, or Ca2+.
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Word Map
- 4.3.1.16
- l-erythro-3-hydroxyaspartate
- pyridoxal
- racemase
- protein-1
- threonine
- delftia
-
micromol
-
fold-type
-
soil-isolated
- chicken
- 5'-phosphate
- pombe
- hydroxylamine
- dehydration
-
5'-phosphate-dependent
- d-serine
- edta
-
schizosaccharomyces
- synthesis
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
d-tha dh, l-threo-3-hydroxyaspartate dehydratase, d-threo-3-hydroxyaspartate dehydratase, l-tha dh, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
L-threo-3-hydroxyaspartate dehydratase
threo-3-hydroxyaspartate ammonia-lyase
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-
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threo-3-hydroxyaspartate dehydratase
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-
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L-threo-3-hydroxyaspartate dehydratase
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-
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L-threo-3-hydroxyaspartate dehydratase
pyridoxal 5'-phosphate-dependent
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
threo-3-hydroxy-L-aspartate = oxaloacetate + NH3
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Deamination
Deamination
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-
-
-
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SYSTEMATIC NAME
IUBMB Comments
threo-3-hydroxy-L-aspartate ammonia-lyase (oxaloacetate-forming)
A pyridoxal-phosphate protein. The enzyme, purified from the bacterium Pseudomonas sp. T62, is highly specific, and does not accept any other stereoisomer of 3-hydroxyaspartate. Different from EC 4.3.1.20, erythro-3-hydroxy-L-aspartate ammonia-lyase and EC 4.3.1.27, threo-3-hydroxy-D-aspartate ammonia-lyase. Requires a divalent cation such as Mn2+, Mg2+, or Ca2+.
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CAS REGISTRY NUMBER
COMMENTARY
248270-70-4
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-threo-3-hydroxyaspartate
oxaloacetate + NH3
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no substrates are D-threo or D,L-erythro-3-hydroxyaspartate
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?
additional information
?
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no activity with erythro-3-hydroxy-L-aspartate and threo-3-hydroxy-D-aspartate
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-
?
additional information
?
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none of the other 3-hydroxy amino acids tested (DL-erythro- and D-threo-3-hydroxyaspartate, D-threonine, L-threonine, DL-allo-threonine, D-serine, L-serine, and DL-phenylserine) is a substrate for this enzyme, either at 5 mM or 50 mM, as in the case of the enzyme from the original strain
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-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
none of the other 3-hydroxy amino acids tested (DL-erythro- and D-threo-3-hydroxyaspartate, D-threonine, L-threonine, DL-allo-threonine, D-serine, L-serine, and DL-phenylserine) is a substrate for this enzyme, either at 5 mM or 50 mM, as in the case of the enzyme from the original strain
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-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Mg2+
Mn2+
Ca2+
By addition of 1 mM to the reaction mixture, relative enzyme activity increased to 159% of control activity.
Mg2+
By addition of 1 mM to the reaction mixture, relative enzyme activity increased to 196% of control activity.
Mn2+
By addition of 1 mM to the reaction mixture, relative enzyme activity increased to 151% of control activity.
Mn2+
effect of divalent cations are measured using the enzyme as control dialyzed against the buffer minus MnCl2, showing a decrease of the specific activity of the enzyme to approximately 36% of the initial activity after overnight dialysis
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ATP
addition of 10 mM decreases enzyme activity to 89% of the control
CoCl2
1 mM causes inhibition enzyme activity (81% relative activity)
CuCl2
1 mM causes inhibition enzyme activity (92% relative activity)
GDP
addition of 10 mM decreases enzyme activity to 73% of the control
L-erythro-3-hydroxyaspartate
5 mM, decrease the enzyme activity to 15%
SnCl2
1 mM causes inhibition enzyme activity (70% relative activity)
ZnCl2
1 mM causes inhibition enzyme activity (56% relative activity)
EDTA
strong inhibition by EDTA (69% inhibition), suggesting that metal ions are involved in the enzyme reaction
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ADP
addition of 10 mM increases enzyme activity to 106% of the control
AMP
addition of 10 mM increases enzyme activity to 144% of the control
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Dehydration
Crystallization and preliminary X-ray diffraction studies of D-threo-3-hydroxyaspartate dehydratase isolated from Delftia sp. HT23.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.27
erythro-3-hydroxy-D-aspartate
pH and temperature not specified in the publication
0.57
threo-3-hydroxy-L-aspartate
pH and temperature not specified in the publication
additional information
additional information
none of the other 3-hydroxy amino acids tested (DL-erythro- and D-threo-3-hydroxyaspartate, D-threonine, L-threonine, DL-allo-threonine, D-serine, L-serine, and DL-phenylserine) is a substrate for this enzyme, either at 5 mM or 50 mM, as in the case of the enzyme from the original strain
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0.54
L-threo-3-hydroxyaspartate
exhibits dehydratase activity specific only to L-threo-3-hydroxyaspartate
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.19
erythro-3-hydroxy-D-aspartate
pH and temperature not specified in the publication
8.61
threo-3-hydroxy-L-aspartate
pH and temperature not specified in the publication
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
8.01
erythro-3-hydroxy-D-aspartate
pH and temperature not specified in the publication
15.2
threo-3-hydroxy-L-aspartate
pH and temperature not specified in the publication
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
DL-aspartate, L-serine, DL-threonine, DL-allo-threonine, DL-phenylserine, or malonic acid did not cause significant inhibition of the enzyme reaction at 5 mM
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
exhibits no detectable serine/aspartate racemase activity
additional information
K53A mutant enzyme shows no detectable activity
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Show AA Sequence and Transmembrane Helices (1107 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
36000
determined by using a MALDI-TOF mass spectrometer, measured value is lower than that determined by sodium dodecyl sulfate polyacrylamide gel electrophoresis (40 kDa), and that of the enzyme purified from the original strain (approximately 39 kDa by SDS-PAGE). The discrepancy may be due to the surface charge of the protein or some unknown factors such as the conformation of the enzyme
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
SDS-PAGE analysis shows 39000 subunit, either monomer or dimer
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystals of D-THA DH belong to space group I4(1)22, with unit-cell parameters a = b = 157.3, c = 157.9 A. Single wavelength anomalous diffraction data are collected to a resolution of 2.0 A
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
after centrifugation of cultivated cell culture with the recombinant enzyme, resulting supernatant is applied to a Ni-sepharose column connected to a fast protein liquid chromatography system. The column is equilibrated with buffer supplemented with 20 mM imidazole. The enzyme is eluted with imidazole gradient.
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpression of recombinant D-THA DH is carried out using a Rhodococcus erythropolis expression system
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the gene encoding L-THA DH is cloned and expressed in Escherichia coli
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
the recombinant enzyme expressed in Escherichia coli is used to produce optically pure L-erythro-3-hydroxyaspartate and D-threo-3-hydroxyaspartate from the corresponding DL-racemic mixtures
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wada, M.; Matsumoto, T.; Nakamori, S.; Sakamoto, M.; Kataoka, M.; Liu, J.Q.; Itoh, N.; Yamada, H.; Shimizu, S.
Purification and characterization of a novel enzyme, L-threo-3-hydroxyaspartate dehydratase, from Pseudomonas sp. T62
FEMS Microbiol. Lett.
179
147-151
1999
Pseudomonas sp.
brenda
Murakami, T.; Maeda, T.; Yokota, A.; Wada, M.
Gene cloning and expression of pyridoxal 5-phosphate-dependent L-threo-3-hydroxyaspartate dehydratase from Pseudomonas sp. T62, and characterization of the recombinant enzyme
J. Biochem.
145
661-668
2009
Pseudomonas sp. T62 (A4F2N8)
brenda
Matsumoto, Y.; Yasutake, Y.; Takeda, Y.; Tamura, T.; Yokota, A.; Wada, M.
Crystallization and preliminary X-ray diffraction studies of D-threo-3-hydroxyaspartate dehydratase isolated from Delftia sp. HT23
Acta Crystallogr. Sect. F
69
1131-1134
2013
Delftia sp.
brenda
Nagano, H.; Shibano, K.; Matsumoto, Y.; Yokota, A.; Wada, M.
Isolation and amino acid sequence of a dehydratase acting on D-erythro-3-hydroxyaspartate from Pseudomonas sp. N99, and its application in the production of optically active 3-hydroxyaspartate
Biosci. Biotechnol. Biochem.
81
1156-1164
2017
Pseudomonas sp. N99 (L0N5C4)
brenda
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