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

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The enzyme appears in viruses and cellular organisms

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EC NUMBER
COMMENTARY hide
4.2.1.43
-
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RECOMMENDED NAME
GeneOntology No.
2-dehydro-3-deoxy-L-arabinonate dehydratase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2-dehydro-3-deoxy-L-arabinonate = 2,5-dioxopentanoate + H2O
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
elimination
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
L-arabinose degradation III
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-
L-lyxonate degradation
-
-
d-xylose degradation
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degradation of pentoses
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Ascorbate and aldarate metabolism
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-
Metabolic pathways
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-
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SYSTEMATIC NAME
IUBMB Comments
2-dehydro-3-deoxy-L-arabinonate hydro-lyase (2,5-dioxopentanoate-forming)
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CAS REGISTRY NUMBER
COMMENTARY hide
37263-10-8
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MNF300
-
-
Manually annotated by BRENDA team
NGR234
-
-
Manually annotated by BRENDA team
NGR234
-
-
Manually annotated by BRENDA team
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
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
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-oxobutanoate
-
-
DL-2-keto-3-hydroxypentanoate
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-
p-hydroxymercuribenzoate
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.07
2-dehydro-3-deoxy-L-arabinonate
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-
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4
p-hydroxymercuribenzoate
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-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.8 - 9.2
-
less than 50% of maximal activity above and below
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Azospirillum brasilense;
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35000
-
2 * 35000, SDS-PAGE
36000
-
2 * 36000, SDS-PAGE
84800
-
gel filtration
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
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
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 10 mM phosphate buffer, pH 7.5, 20% (NH4)2SO4
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
wild-type and mutant enzymes Q143N, Q143E, Q143S, Q143T, and Q143Y
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed as a N-terminal His6-tagged protein in Escherichia coli
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mutant enzymes Q143N, Q143E, Q143S, Q143T, and Q143Y are overexpressed in Escherichia coli cells as a His6-tagged enzyme
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Q143E
-
inactive mutant enzyme
Q143N
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inactive mutant enzyme
Q143S
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inactive mutant enzyme
Q143T
-
inactive mutant enzyme
Q143Y
-
inactive mutant enzyme
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Show AA Sequence (101 entries)
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LINKS TO OTHER DATABASES (specific for EC-Number 4.2.1.43)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)