Information on EC 4.2.1.43 - 2-dehydro-3-deoxy-L-arabinonate dehydratase

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The expected taxonomic range for this enzyme is: Proteobacteria

EC NUMBER
COMMENTARY
4.2.1.43
-
RECOMMENDED NAME
GeneOntology No.
2-dehydro-3-deoxy-L-arabinonate dehydratase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
2-dehydro-3-deoxy-L-arabinonate = 2,5-dioxopentanoate + H2O
show the reaction diagram
-
-
-
-
2-dehydro-3-deoxy-L-arabinonate = 2,5-dioxopentanoate + H2O
show the reaction diagram
Schiff base intermediate
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
elimination
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Ascorbate and aldarate metabolism
-
L-arabinose degradation III
-
Metabolic pathways
-
SYSTEMATIC NAME
IUBMB Comments
2-dehydro-3-deoxy-L-arabinonate hydro-lyase (2,5-dioxopentanoate-forming)
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
2-keto-3-deoxy-L-arabinonate dehydratase
-
-
-
-
dehydratase, 2-keto-3-deoxyL-arabonate
-
-
-
-
KDA dehydratase
-
-
-
-
L-2-keto-3-deoxyarabonate dehydratase
-
-
-
-
L-2-keto-3-deoxyarabonate dehydratase
Q1JUQ0
-
L-KDA dehydratase
Q1JUQ0
-
CAS REGISTRY NUMBER
COMMENTARY
37263-10-8
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
Rhizobium leguminosarum MNF300
MNF300
-
-
Manually annotated by BRENDA team
NGR234
-
-
Manually annotated by BRENDA team
Rhizobium sp. NGR234
NGR234
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-dehydro-3-deoxy-L-arabinonate
2,5-dioxopentanoate + H2O
show the reaction diagram
-
-
-
-
-
L-2-keto-3-deoxyarabonate
2-oxoglutarate semialdehyde + H2O
show the reaction diagram
-
-
-
-
L-2-keto-3-deoxyarabonate
2-oxoglutarate semialdehyde + H2O
show the reaction diagram
-
-
-
-
L-2-keto-3-deoxyarabonate
2-oxoglutarate semialdehyde + H2O
show the reaction diagram
-
-
-
?
L-2-keto-3-deoxyarabonate
2-oxoglutarate semialdehyde + H2O
show the reaction diagram
-
-
-
-
?
L-2-keto-3-deoxyarabonate
2-oxoglutarate semialdehyde + H2O
show the reaction diagram
-
-
-
-
?
L-2-keto-3-deoxyarabonate
2-oxoglutarate semialdehyde + H2O
show the reaction diagram
Rhizobium leguminosarum MNF 300, Rhizobium leguminosarum MNF300, Rhizobium sp. NGR234, Rhizobium sp. NGR
-
-
-
-
?
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
DL-2-keto-3-hydroxypentanoate
-
-
p-hydroxymercuribenzoate
-
-
p-hydroxymercuribenzoate
-
4 mM, 50% inhibition
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.07
-
2-dehydro-3-deoxy-L-arabinonate
-
-
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
4
-
p-hydroxymercuribenzoate
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.8
9.2
-
less than 50% of maximal activity above and below
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
84800
-
-
gel filtration
85000
-
-
gel filtration
85000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
dimer
-
2 * 36000, SDS-PAGE
dimer
-
2 * 35000, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
crystallized at 18°C using the hanging-drop vapour-diffusion method. The crystal diffracts to 2.0 A resolution using synchrotron radiation and belongs to the trigonal space group P3(1)2(1) or its enantiomorph P3(2)2(1), with unit-cell parameters a = b = 78.91, c = 207.71 A
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
4°C, 10 mM phosphate buffer, pH 7.5, 20% (NH4)2SO4
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
wild-type and mutant enzymes Q143N, Q143E, Q143S, Q143T, and Q143Y
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expressed as a N-terminal His6-tagged protein in Escherichia coli
-
mutant enzymes Q143N, Q143E, Q143S, Q143T, and Q143Y are overexpressed in Escherichia coli cells as a His6-tagged enzyme
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Q143E
-
inactive mutant enzyme
Q143N
-
inactive mutant enzyme
Q143S
-
inactive mutant enzyme
Q143T
-
inactive mutant enzyme
Q143Y
-
inactive mutant enzyme