BRENDA - Enzyme Database
show all sequences of 4.2.1.82

The crystal structure of D-xylonate dehydratase reveals functional features of enzymes from the Ilv/ED dehydratase family

Rahman, M.M.; Andberg, M.; Koivula, A.; Rouvinen, J.; Hakulinen, N.; Sci. Rep. 8, 865 (2018)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
heterologously expressed in Escherichia coli
Caulobacter vibrioides
Crystallization (Commentary)
Crystallization
Organism
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
Caulobacter vibrioides
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
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
Caulobacter vibrioides
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Caulobacter vibrioides
Q9A9Z2
-
-
Caulobacter vibrioides ATCC 19089
Q9A9Z2
-
-
Purification (Commentary)
Commentary
Organism
-
Caulobacter vibrioides
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-xylonate
-
749370
Caulobacter vibrioides
2-dehydro-3-deoxy-D-xylonate + H2O
-
-
-
?
D-xylonate
-
749370
Caulobacter vibrioides ATCC 19089
2-dehydro-3-deoxy-D-xylonate + H2O
-
-
-
?
Subunits
Subunits
Commentary
Organism
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
Caulobacter vibrioides
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
30
-
assay at
Caulobacter vibrioides
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
assay at
Caulobacter vibrioides
Cofactor
Cofactor
Commentary
Organism
Structure
[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
Caulobacter vibrioides
Cloned(Commentary) (protein specific)
Commentary
Organism
heterologously expressed in Escherichia coli
Caulobacter vibrioides
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
[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
Caulobacter vibrioides
Crystallization (Commentary) (protein specific)
Crystallization
Organism
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
Caulobacter vibrioides
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
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
Caulobacter vibrioides
Purification (Commentary) (protein specific)
Commentary
Organism
-
Caulobacter vibrioides
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-xylonate
-
749370
Caulobacter vibrioides
2-dehydro-3-deoxy-D-xylonate + H2O
-
-
-
?
D-xylonate
-
749370
Caulobacter vibrioides ATCC 19089
2-dehydro-3-deoxy-D-xylonate + H2O
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
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
Caulobacter vibrioides
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
30
-
assay at
Caulobacter vibrioides
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
assay at
Caulobacter vibrioides
Other publictions for EC 4.2.1.82
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
749370
Rahman
The crystal structure of D-xy ...
Caulobacter vibrioides, Caulobacter vibrioides ATCC 19089
Sci. Rep.
8
865
2018
-
-
1
1
-
-
-
-
-
1
-
-
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4
-
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1
-
-
-
-
-
2
1
1
-
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1
-
-
1
-
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-
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1
1
1
-
-
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-
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-
1
-
-
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1
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2
1
1
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1
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746662
Rahman
Crystallization and X-ray dif ...
Caulobacter vibrioides, Caulobacter vibrioides ATCC 19089
Acta Crystallogr. Sect. F
72
604-608
2016
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-
1
1
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-
-
-
-
-
-
2
-
6
-
-
1
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-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
-
2
-
-
-
1
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
747219
Jiang
Characterization of D-xylonat ...
Escherichia coli, Escherichia coli K12
Bioengineered
6
227-232
2015
-
-
-
-
-
-
4
1
-
2
1
2
-
3
-
-
1
-
-
-
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-
2
-
1
1
1
-
1
1
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-
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-
4
-
1
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2
1
2
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-
1
-
-
-
-
2
-
1
1
1
-
1
1
-
-
-
-
-
-
-
-
698940
Johnsen
D-xylose degradation pathway i ...
Haloferax volcanii
J. Biol. Chem.
284
27290-27303
2009
1
-
1
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-
2
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1
3
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10
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1
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1
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3
1
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1
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1
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2
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1
3
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1
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1
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3
1
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1
1
-
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-
701792
Meijnen
Establishment of oxidative D-x ...
Caulobacter vibrioides
Appl. Environ. Microbiol.
75
2784-2791
2009
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1
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1
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5
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1
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1
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1
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1
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1
1
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648798
Dahms
D-xylo-aldonate dehydratase ...
Pseudomonas sp., Pseudomonas sp. MSU-1
Methods Enzymol.
90
302-305
1982
1
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-
-
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2
2
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6
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2
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8
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1
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1
1
8
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1
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2
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1
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1
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2
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2
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6
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2
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1
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1
1
8
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1
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2
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1
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