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Information on EC 4.3.1.27 - threo-3-hydroxy-D-aspartate ammonia-lyase
for references in articles please use BRENDA:EC4.3.1.27
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EC Tree 4 Lyases
4.3 Carbon-nitrogen lyases
4.3.1 Ammonia-lyases
4.3.1.27 threo-3-hydroxy-D-aspartate ammonia-lyase
IUBMB Comments
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+.
The expected taxonomic range for this enzyme is: Bacteria, Archaea
showSynonyms
D-THA DH, D-threo-3-hydroxyaspartate ammonia-lyase, D-threo-3-hydroxyaspartate dehydratase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
D-THA DH
D-threo-3-hydroxyaspartate dehydratase
D-threo-3-hydroxyaspartate dehydratase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
threo-3-hydroxy-D-aspartate = oxaloacetate + NH3
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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+.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-threo-3-hydroxyaspartate
oxaloacetate + NH3
Substrates: -
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L-threo-3-hydroxyaspartate
oxaloacetate + NH3
Substrates: -
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?
threo-3-hydroxy-D-aspartate
oxaloacetate + NH3
Substrates: the substrate specificity of the enzyme is determined by the orientation of the Cbeta-OH at the active site, whose spatial arrangement is compatible with the 3R configuration of 3-hydroxyaspartate. The enzyme also catalyzes the dehydration of erythro-3-hydroxy-L-aspartate
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additional information
?
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Substrates: D-erythro-3-hydroxyaspartate is not a substrate
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?
additional information
?
-
Substrates: the purified enzyme shows no alanine racemase activity
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
one Mg2+ is located between His351 and Cys353 at the active site. The other Mg2+ is chelated by the beta-carboxyl O atom and the beta-hydroxyl O atom of erythro-3-hydroxy-D-aspartate, forming a erythro-3-hydroxy-D-aspartate-Mg2+ complex
additional information
no activity is detected when Sn2+ or Cu2+ is added
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
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)
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.12
pH 8.0, 30°C, mutant enzyme H351A, substrate: threo-3-hydroxy-D-aspartate
21.1
pH 8.0, 30°C, wild-type enzyme, substrate: threo-3-hydroxy-D-aspartate
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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
Highest Expressing Human Cell Lines
Cell Line Links Show AA Sequence and Transmembrane Helices (165 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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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40900
calculated from the deduced amino acid sequence of the recombinant enzyme
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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
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sitting drop or hanging drop vapor diffusion method at 20°C, crystal structures of the enzyme in complex with the inhibitor D-erythro-3-hydroxyaspartate, crystal structure of the poorly active H351A mutant complexed with its substrate L-erythro-3-hydroxyaspartate, and H351A mutant enzyme complexed with the reaction intermediate 2-amino maleic acid
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C353A
mutations significantly decreases the activity toward threo-3-hydroxy-D-aspartate and erythro-3-hydroxy-L-aspartate
H351A
mutations significantly decreases the activity toward threo-3-hydroxy-D-aspartate and erythro-3-hydroxy-L-aspartate
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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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
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the enzyme is not induced by D-serine, D-threonine, D-aspartate, or peptone
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
optically pure synthesis of L-threo-3-hydroxyaspartate and D-threo-3-hydroxyaspartate, promising intermediates for the synthesis of beta-benzyloxyaspartate by using a purified enzyme as a biocatalyst for the resolution of racemic DL-threo-3-hydroxyaspartate and DL-erythro-3-hydroxyaspartate. Considering 50% of the theoretical maximum, efficient yields of L-threo-3-hydroxyaspartate (38.9 %) and D-erythro-3-hydroxyaspartate (48.9 %) as isolated crystals are achieved with more than 99 % enantiomeric excess
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Maeda, T.; Takeda, Y.; Murakami, T.; Yokota, A.; Wada, M.
Purification, characterization and amino acid sequence of a novel enzyme, D-threo-3-hydroxyaspartate dehydratase, from Delftia sp. HT23
J. Biochem.
148
705-712
2010
Delftia sp. HT23 (B2DFG5)
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
Matsumoto, Y.; Yasutake, Y.; Takeda, Y.; Tamura, T.; Yokota, A.; Wada, M.
Structural insights into the substrate stereospecificity of D-threo-3-hydroxyaspartate dehydratase from Delftia sp. HT23 a useful enzyme for the synthesis of optically pure L-threo- and D-erythro-3-hydroxyaspartate
Appl. Microbiol. Biotechnol.
99
7137-7150
2015
Delftia sp. HT23 (B2DFG5)
brenda
EXTERNAL LINKS (specific for EC-Number 4.3.1.27)
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Release 2023.1 (January 2023)
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