Information on EC 4.2.1.82 - xylonate dehydratase

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

EC NUMBER
COMMENTARY hide
4.2.1.82
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RECOMMENDED NAME
GeneOntology No.
xylonate dehydratase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
D-xylonate = 2-dehydro-3-deoxy-D-xylonate + H2O
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C-O bond cleavage by elimination of water
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
ethylene glycol biosynthesis (engineered)
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Pentose and glucuronate interconversions
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xylose degradation III
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xylose degradation IV
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d-xylose degradation
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SYSTEMATIC NAME
IUBMB Comments
D-xylonate hydro-lyase (2-dehydro-3-deoxy-D-xylonate-forming)
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CAS REGISTRY NUMBER
COMMENTARY hide
84788-77-2
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
strain MSU-1
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Manually annotated by BRENDA team
strain MSU-1
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
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is essential for establishing an oxidative D-xylose catabolic pathway in Pseudomonas putida S12, but coexpression of the putative 2-keto-3-deoxy-D-xylonate dehydratase (XylX) improves the biomass yield by approximately 10%, while the growth rate is not altered. When XylA, catalyzing the next and final step in the pathway, is also coexpressed, both the biomass yield and the maximum growth rate increase. Lower-pathway activities of strains S12xylXD and S12xylD, which rely on endogenous semialdehyde dehydrogenase, are about one-half the activity of the strain that coexpresses the alpha-KGSA dehydrogenase (S12xylXAD)
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-gluconate
2-dehydro-3-deoxy-D-gluconate + H2O
show the reaction diagram
D-xylonate
2-dehydro-3-deoxy-D-xylonate + H2O
show the reaction diagram
D-xylose
2-dehydro-3-deoxy-D-xylonate + H2O
show the reaction diagram
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?
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
additional information
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
FeSO4
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addition of 5 mM to the EDTA-inhibited enzyme results in 75% of the original activity
MgCl2
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addition of 5 mM to the EDTA-inhibited enzyme results in 100% of the original activity
MgSO4
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addition of 5 mM to the EDTA-inhibited enzyme results in 100% of the original activity
Mn2+
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addition of 5 mM to the EDTA-inhibited enzyme results in 13% of the original activity
PbCl2
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addition of 5 mM to the EDTA-inhibited enzyme results in 50% of the original activity
additional information
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absolute requirement for a divalent cation, no reactivation of EDTA-inhibited enzyme by CuSO4, CoCl2, ZnSO4 and NiCl2, all at 5 mM
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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not inhibited by thiols, iodoacetic acid, p-mercuribenzoate or N-ethylmaleimide, all at 2 mM
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
xylose
xylonate dehydratase activity is induced 2fold in xylose-grown cells
additional information
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enzyme is induced by growth on D-xylose, but not by D-gluconate, D-glucose, L-arabinose or D-fucose
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.4 - 2.77
D-gluconate
0.55 - 2.98
D-xylonate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1.1
100fold purified enzyme, with D-xylonate or D-gluconate as substrate
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
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in 50 mM Bicine
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 30
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assay at
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45500
8 * 45500, sequence analysis. 8 * 52000, gel filtration
52000
8 * 45500, sequence analysis. 8 * 52000, gel filtration
340000
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homooctamer
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
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half-life: 14 min
70
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half-life: 2 min
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
frozen state, several months, stable
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
by centrifugation, gel filtration, ammonium sulfate precipitation and ultrafiltration, 100fold. Recombinant XAD purified by Ni-NTA chromatography
partial, 21fold
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
PCR product cloned into pET19b. The resulting plasmid harvested from Escherichia coli JM109, sequenced, and transformed into Escherichia coli Rosetta(DE3)-pLysS expression strain. In-frame deletion mutant amplified and ligated into pTA131, sequenced, and transformed in Haloferax volcanii H26 DELTApyrE2
xylXABCD, xylXAD, xylXD, xylD or xylX ligated into the vector pJTmcs using the KpnI, XbaI, and XmaJI restriction sites, under the control of the constitutive tac promoter, expressed in Pseudomonas putida S12
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