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

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Mark a special word or phrase in this record:
Search Reference ID:
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Proteobacteria

EC NUMBER
COMMENTARY hide
4.2.1.43
-
RECOMMENDED NAME
GeneOntology No.
2-dehydro-3-deoxy-L-arabinonate dehydratase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2-dehydro-3-deoxy-L-arabinonate = 2,5-dioxopentanoate + H2O
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
elimination
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Ascorbate and aldarate metabolism
-
-
d-xylose degradation
-
-
degradation of pentoses
-
-
L-arabinose degradation III
-
-
L-lyxonate degradation
-
-
Metabolic pathways
-
-
SYSTEMATIC NAME
IUBMB Comments
2-dehydro-3-deoxy-L-arabinonate hydro-lyase (2,5-dioxopentanoate-forming)
-
CAS REGISTRY NUMBER
COMMENTARY hide
37263-10-8
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MNF300
-
-
Manually annotated by BRENDA team
MNF300
-
-
Manually annotated by BRENDA team
NGR234
-
-
Manually annotated by BRENDA team
NGR234
-
-
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
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
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-oxobutanoate
-
-
DL-2-keto-3-hydroxypentanoate
-
-
p-hydroxymercuribenzoate
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.07
2-dehydro-3-deoxy-L-arabinonate
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4
p-hydroxymercuribenzoate
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.8 - 9.2
-
less than 50% of maximal activity above and below
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
84800
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 10 mM phosphate buffer, pH 7.5, 20% (NH4)2SO4
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
wild-type and mutant enzymes Q143N, Q143E, Q143S, Q143T, and Q143Y
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
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
COMMENTARY hide
LITERATURE
Q143E
-
inactive mutant enzyme
Q143N
-
inactive mutant enzyme
Q143S
-
inactive mutant enzyme
Q143T
-
inactive mutant enzyme
Q143Y
-
inactive mutant enzyme