Information on EC 4.3.1.20 - erythro-3-hydroxy-L-aspartate ammonia-lyase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
4.3.1.20
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RECOMMENDED NAME
GeneOntology No.
erythro-3-hydroxy-L-aspartate ammonia-lyase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
erythro-3-hydroxy-L-aspartate = oxaloacetate + NH3
show the reaction diagram
A pyridoxal-phosphate protein.; A pyridoxal-phosphate protein. The reaction catalysed probably involves initial elimination of water, hence the enzyme's original classification as EC 4.2.1.38, erythro-3-hydroxyaspartate dehydratase, followed by isomerization and hydrolysis of the product with C-N bond breakage
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
elimination
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
glycolate and glyoxylate degradation III
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SYSTEMATIC NAME
IUBMB Comments
erythro-3-hydroxy-L-aspartate ammonia-lyase (oxaloacetate-forming)
A pyridoxal-phosphate protein. The enzyme, which was characterized from the bacterium Paracoccus denitrificans NCIMB 8944, is highly specific for the L-isomer of erythro-3-hydroxyaspartate. Different from EC 4.3.1.16, threo-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+, and Ca2+.
CAS REGISTRY NUMBER
COMMENTARY hide
37290-74-7
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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-
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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
Erythro-3-hydroxyaspartate
?
show the reaction diagram
Erythro-DL-beta-hydroxyaspartate
Oxaloacetate + NH3
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
Erythro-3-hydroxyaspartate
?
show the reaction diagram
additional information
?
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hydroxyaspartate dehydratase and aconitase activities reside on the same protein and at a common active site
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mn2+
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restores activity after EDTA treatment
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-Pyridinecarboxylic acid
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Maleate
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competitive
p-chloromercuribenzoate
Semicarbazide
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.43
erythro-L-beta-hydroxyaspartate
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additional information
additional information
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Km-value varied with pH, optimum at pH 7.8
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
-
Manually annotated by BRENDA team
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 10
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rapid loss of activity below pH 6 and above pH 10
210866
7.5 - 9.5
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most stable
210866
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-15°C, with 0.01M Tris-HCl buffer, pH 8, 1 mM MgCl2 and 0.01 mM pyridoxal 5'-phosphate, 50% loss of activity in 60 days
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2°C, with 0.01M Tris-HCl buffer, pH 8, 1 mM MgCl2 and 0.01 mM pyridoxal 5'-phosphate, 50% loss of activity in 10 days
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE