Information on EC 4.1.3.B3 - 4-carboxy-4-hydroxy-2-oxoadipate aldolase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
4.1.3.B3
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
4-carboxy-4-hydroxy-2-oxoadipate aldolase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
4-carboxy-4-hydroxy-2-oxoadipate = oxaloacetate + pyruvate
show the reaction diagram
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-
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SYSTEMATIC NAME
IUBMB Comments
4-carboxy-4-hydroxy-2-oxoadipate pyruvate lyase (pyruvate-forming)
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene pmdF
UniProt
Manually annotated by BRENDA team
gene pmdF
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
metabolism
additional information
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the Pseudomonas putida F1 HMG/CHA aldolase has a D-X20-R-D motif, active site structure, structure-function relationship, overview. The Glu199 residue in HMG/CHA aldolase positions one water molecule and in concert with the Asp102 residue positions a second water molecule that coordinate with the bound magnesium ion
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-carboxy-4-hydroxy-2-oxoadipate
oxaloacetate + pyruvate
show the reaction diagram
4-carboxy-4-hydroxy-2-oxoadipate
pyruvate + oxaloacetate
show the reaction diagram
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-
-
r
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
4-carboxy-4-hydroxy-2-oxoadipate
oxaloacetate + pyruvate
show the reaction diagram
additional information
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
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required
additional information
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the enzyme is a class II divalent metal ion-dependent aldolase. Coordination of a metal ion to support the binding of a pyruvyl moiety in the class II aldolase is essential, metal binding Glu199 residue
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
oxalate
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competitive inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.03 - 0.066
4-carboxy-4-hydroxy-2-oxoadipate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
7.5 - 14.4
4-carboxy-4-hydroxy-2-oxoadipate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
220 - 250
4-carboxy-4-hydroxy-2-oxoadipate
10523
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37.7
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wild type protein, pH 8.0, 25°C
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
assay at room temperature
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
26000
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6 * 26000, crystal structure, gel filtration and SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homohexamer
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6 * 26000, crystal structure, gel filtration and SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop method, PEG 4000
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, 20 mM sodium HEPES buffer, pH7.5, stable for 2 months
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ion exchange chromatography, hydrophobic interaction chromatography, gel filtration
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recombinant enzyme from Escherichia coli
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(lambdaDE3)
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gene pmdF, orf CtCNB1_2744, DNA and amino acid sequence determination and analysis, genetic organization, phylogenetic analysis, expression in Escherichia coli
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E199A
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site-directed mutagenesis, the mutant shows reduced 4-hydroxy-4-methyl-2-oxoglutarate aldolase and oxaloacetate decarboxylase activities compared to the wild-type enzyme
R123A
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no activity
R123K
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retains some activity (substrate 4-hydroxy-4-methyl-2-oxoglutarate)
additional information