Any feedback?
No. of entries
Information on EC 4.2.1.82 - xylonate dehydratase
for references in articles please use BRENDA:EC4.2.1.82
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
The expected taxonomic range for this enzyme is: Bacteria, Archaea
- 4.2.1.82
-
caulobacter
- crescentus
- d-xylose
- glycol
- biomass
- 1,2,4-butanetriol
- aldolase
- semialdehyde
- pentose
- putida
-
2-keto
- ethylene
- dehydration
-
azospirillum
-
leguminosarum
-
halophilic
-
dahms
- alpha-ketoglutarate
-
haloferax
-
lactococcus
-
rhizobium
- fe-s
- 6-phosphogluconate
-
2-ketoacid
-
four-step
-
pentonate
- trifolii
- volcanii
- brasilense
- lactis
showSynonyms
d-xylonate dehydratase, xylonate dehydratase, ccxydht, more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CcXyDHT
D-xylo-aldonate dehydratase
-
-
-
-
D-xylonate dehydratase
dehydratase, D-xylonate
-
-
-
-
XYLD
YjhG
D-xylonate dehydratase
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
D-xylonate = 2-dehydro-3-deoxy-D-arabinonate + H2O
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C-O bond cleavage by elimination of water
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
D-xylose degradation III, D-xylose degradation IV, D-xylose degradation to ethylene glycol (engineered), D-xylose degradation V, D-xylose degradation VI
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
D-xylonate hydro-lyase (2-dehydro-3-deoxy-D-xylonate-forming)
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
84788-77-2
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-xylose
2-dehydro-3-deoxy-D-xylonate + H2O
-
Substrates: -
Products: -
Products: -
?
D-gluconate
2-dehydro-3-deoxy-D-gluconate + H2O
Substrates: XAD catalyzes the dehydration of D-gluconate at a similar catalytic efficiency as compared with D-xylonate
Products: -
Products: -
?
D-gluconate
2-dehydro-3-deoxy-D-gluconate + H2O
-
Substrates: at 55% of the rate with D-xylonate
Products: -
Products: -
?
D-gluconate
2-dehydro-3-deoxy-D-gluconate + H2O
-
Substrates: at 55% of the rate with D-xylonate
Products: -
Products: -
?
D-xylonate
2-dehydro-3-deoxy-D-arabinonate + H2O
Substrates: the enzyme is involved in a nonphosphorylative oxidation pathway of pentose sugars
Products: -
Products: -
?
D-xylonate
2-dehydro-3-deoxy-D-arabinonate + H2O
Substrates: -
Products: -
Products: -
?
D-xylonate
2-dehydro-3-deoxy-D-arabinonate + H2O
-
Substrates: -
Products: -
Products: -
?
D-xylonate
2-dehydro-3-deoxy-D-arabinonate + H2O
Substrates: the enzyme is involved in a nonphosphorylative oxidation pathway of pentose sugars
Products: -
Products: -
?
D-xylonate
2-dehydro-3-deoxy-D-arabinonate + H2O
Substrates: -
Products: -
Products: -
?
D-xylonate
2-dehydro-3-deoxy-D-arabinonate + H2O
Substrates: -
Products: -
Products: -
?
D-xylonate
2-dehydro-3-deoxy-D-arabinonate + H2O
Substrates: -
Products: -
Products: -
?
D-xylonate
2-dehydro-3-deoxy-D-arabinonate + H2O
Substrates: XAD catalyzes the dehydration of D-xylonate at a similar catalytic efficiency as compared with D-gluconate
Products: -
Products: -
?
D-xylonate
2-dehydro-3-deoxy-D-arabinonate + H2O
-
Substrates: -
Products: -
Products: -
?
D-xylonate
2-dehydro-3-deoxy-D-arabinonate + H2O
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
Substrates: D-galactonate is not utilized
Products: -
Products: -
?
additional information
?
-
-
Substrates: D-galactonate is not utilized
Products: -
Products: -
?
additional information
?
-
-
Substrates: not: D- and L-arabonate, D- and L-fuconate, 6-iodo-6-deoxygalactonate, D- and L-mannonate, D- and L-galactonate, L-gluconate, D-ribonate, D-glucuronate, D-galacturonate, D-galactarate
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme functions in the metabolism of D-xylose, but is probably not operative in glucose/gluconate metabolism
Products: -
Products: -
?
additional information
?
-
-
Substrates: not: D- and L-arabonate, D- and L-fuconate, 6-iodo-6-deoxygalactonate, D- and L-mannonate, D- and L-galactonate, L-gluconate, D-ribonate, D-glucuronate, D-galacturonate, D-galactarate
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme functions in the metabolism of D-xylose, but is probably not operative in glucose/gluconate metabolism
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-xylonate
2-dehydro-3-deoxy-D-arabinonate + H2O
Substrates: the enzyme is involved in a nonphosphorylative oxidation pathway of pentose sugars
Products: -
Products: -
?
D-xylonate
2-dehydro-3-deoxy-D-arabinonate + H2O
Substrates: the enzyme is involved in a nonphosphorylative oxidation pathway of pentose sugars
Products: -
Products: -
?
D-xylonate
2-dehydro-3-deoxy-D-arabinonate + H2O
Substrates: -
Products: -
Products: -
?
D-xylonate
2-dehydro-3-deoxy-D-arabinonate + H2O
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme functions in the metabolism of D-xylose, but is probably not operative in glucose/gluconate metabolism
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme functions in the metabolism of D-xylose, but is probably not operative in glucose/gluconate metabolism
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
[2Fe-2S]-center
each monomer is composed of two domains in which the N-terminal domain forms a binding site for a [2Fe-2S] cluster and a Mg2+ ion
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
FeSO4
-
addition of 5 mM to the EDTA-inhibited enzyme results in 75% of the original activity
Mg2+
MgCl2
-
addition of 5 mM to the EDTA-inhibited enzyme results in 100% of the original activity
MgSO4
-
addition of 5 mM to the EDTA-inhibited enzyme results in 100% of the original activity
Mn2+
PbCl2
-
addition of 5 mM to the EDTA-inhibited enzyme results in 50% of the original activity
additional information
-
absolute requirement for a divalent cation, no reactivation of EDTA-inhibited enzyme by CuSO4, CoCl2, ZnSO4 and NiCl2, all at 5 mM
Mg2+
each monomer is composed of two domains in which the N-terminal domain forms a binding site for a [2Fe-2S] cluster and a Mg2+ ion
Mn2+
-
addition of 5 mM to the EDTA-inhibited enzyme results in 13% of the original activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
not inhibited by thiols, iodoacetic acid, p-mercuribenzoate or N-ethylmaleimide, all at 2 mM
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
xylose
xylonate dehydratase activity is induced 2fold in xylose-grown cells
additional information
-
enzyme is induced by growth on D-xylose, but not by D-gluconate, D-glucose, L-arabinose or D-fucose
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Dehydration
Crystallization and X-ray diffraction analysis of an L-arabinonate dehydratase from Rhizobium leguminosarum bv. trifolii and a D-xylonate dehydratase from Caulobacter crescentus.
Dehydration
In vitro reconstitution and characterisation of the oxidative D-xylose pathway for production of organic acids and alcohols.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.4
D-gluconate
at 42°C, in 0.1 M Tris-HCl buffer, pH 7.5, 2.5 M KCl, 50 mM MgCl2
0.55
D-xylonate
at 42°C, in 0.1 M Tris-HCl buffer, pH 7.5, 2.5 M KCl, 50 mM MgCl2
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1.1
100fold purified enzyme, with D-xylonate or D-gluconate as substrate
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.7 - 8.5
pH 6.7: about 65% of maximal activity, pH 8.5: about 65% of maximal activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 42
20°C: about 60% of maximal activity, 42°C: about 50% of maximal activity, activity is almost undetectable above 60x01C°
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
in-frame deletion mutant has lost its ability to grow on xylose, but it shows the same phenotype as the wild-type during growth on glucose
metabolism
metabolism
-
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)
metabolism
the enzyme is involved in a nonphosphorylative oxidation pathway of pentose sugars
metabolism
-
the enzyme is involved in a nonphosphorylative oxidation pathway of pentose sugars
-
Show AA Sequence and Transmembrane Helices (177 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homooctamer
8 * 45500, sequence analysis. 8 * 52000, gel filtration
tetramer
tetramer
crystallographic data, each monomer is composed of two domains in which the N-terminal domain forms a binding site for a [2Fe-2S] cluster and a Mg2+ ion
tetramer
-
crystallographic data, each monomer is composed of two domains in which the N-terminal domain forms a binding site for a [2Fe-2S] cluster and a Mg2+ ion
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapour-diffusion method at 20°C. Crystals that diffracted to 2.66 A resolution are obtained using sodium formate and polyethylene glycol 3350. They belong to space group C2, with unit-cell parameters a = 270.42, b = 236.13, c = 65.17 A, beta = 97.38°
the crystal structure of D-xylonate dehydratase from Caulobacter crescentus is described at 2.7 A resolution and it is compares with other available enzyme structures from the IlvD/EDD protein family
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
70
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
by centrifugation, gel filtration, ammonium sulfate precipitation and ultrafiltration, 100fold. Recombinant XAD purified by Ni-NTA chromatography
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
heterologously expressed in Escherichia coli
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
construction of a biosynthetic pathway in Escherichia coli to produce 1,2,4-butanetriol from pure D-xylose or corncob hydrolysates. Key steps catalyzed by D-xylonate dehydratase, 2-keto acid decarboxylase and aldehyde reductase are used. The coexpression of these enzymes in recombinant Escherichia coli leads to 1,2,4-butanetriol production of 5.1 g/l under the optimized cultivation conditions. 1,2,4-Butanetriol production from corncob hydrolysates is achieved with a titer of 3.4 g/l
synthesis
construction of in vitro multi-enzyme cascades leading from D-xylose or D-xylonolactone to ethylene glycol, glycolic acid and lactic acid, and simple spectrophotometric assays for the analysis of the efficiency. The dehydration reaction by D-xylonate dehydratase is a rate-limiting step in the pathway. No suitable replacing enzymes are found for this reaction
synthesis
production of 3,4-dihydroxybutyric acid in an engineered Escherichia coli strain expressing glucose dehydrogenase from Bacillus subtilis, D-xylonate dehydratase from E. coli, benzoylformate decarboxylase from Pseudomonas putida and ALDH generates 3.04 g/l 3,4-dihydroxybutyric acid from D-xylose. Disruption of competing pathways by deleting xylA, ghrA, ghrB and adhP contributes to an 87% increase in 3,4-dihydroxybutyric acid accumulation. Expression of a fusion construct containing benzoylformate decarboxylase and D-xylonate dehydratase enhances the 3,4-dihydroxybutyric acid titer to 7.71 g/l, i.e. 0.482 g 3,4-dihydroxybutyric acid/g D-xylose
synthesis
-
construction of a biosynthetic pathway in Escherichia coli to produce 1,2,4-butanetriol from pure D-xylose or corncob hydrolysates. Key steps catalyzed by D-xylonate dehydratase, 2-keto acid decarboxylase and aldehyde reductase are used. The coexpression of these enzymes in recombinant Escherichia coli leads to 1,2,4-butanetriol production of 5.1 g/l under the optimized cultivation conditions. 1,2,4-Butanetriol production from corncob hydrolysates is achieved with a titer of 3.4 g/l
-
synthesis
-
construction of in vitro multi-enzyme cascades leading from D-xylose or D-xylonolactone to ethylene glycol, glycolic acid and lactic acid, and simple spectrophotometric assays for the analysis of the efficiency. The dehydration reaction by D-xylonate dehydratase is a rate-limiting step in the pathway. No suitable replacing enzymes are found for this reaction
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Dahms, A.S.; Donald, A.
D-xylo-aldonate dehydratase
Methods Enzymol.
90
302-305
1982
Pseudomonas sp., Pseudomonas sp. MSU-1
brenda
Johnsen, U.; Dambeck, M.; Zaiss, H.; Fuhrer, T.; Soppa, J.; Sauer, U.; Schoenheit, P.
D-xylose degradation pathway in the halophilic archaeon Haloferax volcanii
J. Biol. Chem.
284
27290-27303
2009
Haloferax volcanii (D4GP40), Haloferax volcanii
brenda
Meijnen, J.P.; de Winde, J.H.; Ruijssenaars, H.J.
Establishment of oxidative D-xylose metabolism in Pseudomonas putida S12
Appl. Environ. Microbiol.
75
2784-2791
2009
Caulobacter vibrioides
brenda
Rahman, M.; Andberg, M.; Koivula, A.; Rouvinen, J.; Hakulinen, N.
Crystallization and X-ray diffraction analysis of an L-arabinonate dehydratase from Rhizobium leguminosarum bv. trifolii and a D-xylonate dehydratase from Caulobacter crescentus
Acta Crystallogr. Sect.F
72
604-608
2016
Caulobacter vibrioides (Q9A9Z2), Caulobacter vibrioides, Caulobacter vibrioides ATCC 19089 (Q9A9Z2)
brenda
Jiang, Y.; Liu, W.; Cheng, T.; Cao, Y.; Zhang, R.; Xian, M.
Characterization of D-xylonate dehydratase YjhG from Escherichia coli
Bioengineered
6
227-232
2015
Escherichia coli (P39358), Escherichia coli, Escherichia coli K12 (P39358)
brenda
Rahman, M.M.; Andberg, M.; Koivula, A.; Rouvinen, J.; Hakulinen, N.
The crystal structure of D-xylonate dehydratase reveals functional features of enzymes from the Ilv/ED dehydratase family
Sci. Rep.
8
865
2018
Caulobacter vibrioides (Q9A9Z2), Caulobacter vibrioides, Caulobacter vibrioides ATCC 19089 (Q9A9Z2)
brenda
Boer, H.; Andberg, M.; Pylkkaenen, R.; Maaheimo, H.; Koivula, A.
In vitro reconstitution and characterisation of the oxidative D-xylose pathway for production of organic acids and alcohols
AMB Express
9
48
2019
Caulobacter vibrioides (Q9A9Z2), Caulobacter vibrioides ATCC 19089 (Q9A9Z2)
brenda
Wang, X.; Xu, N.; Hu, S.; Yang, J.; Gao, Q.; Xu, S.; Chen, K.; Ouyang, P.
D-1,2,4-Butanetriol production from renewable biomass with optimization of synthetic pathway in engineered Escherichia coli
Biores. Technol.
250
406-412
2018
Caulobacter vibrioides (Q9A9Z2), Caulobacter vibrioides ATCC 19089 (Q9A9Z2)
brenda
Liu, Y.; Mao, X.; Zhang, B.; Lin, J.; Wei, D.
Modification of an engineered Escherichia coli by a combinatorial strategy to improve 3,4-dihydroxybutyric acid production
Biotechnol. Lett.
43
2035-2043
2021
Escherichia coli (P77596)
brenda
EXTERNAL LINKS (specific for EC-Number 4.2.1.82)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2026.1 (March 2026)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
![DSMZ Digital Diversity]()
![Global Core Biodata Resource]()
![ELIXIR Core Data Resource]()
![German Network for Bioinformatics Infrastructure]()
