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show all sequences of 1.1.1.122

Crystal structure and biochemical properties of the D-arabinose dehydrogenase from Sulfolobus solfataricus

Brouns, S.J.; Turnbull, A.P.; Willemen, H.L.; Akerboom, J.; van der Oost, J.; J. Mol. Biol. 371, 1249-1260 (2007)

Data extracted from this reference:

Crystallization (Commentary)
Crystallization
Organism
the structure is solved to a resolution of 1.80 A by single-wavelength anomalous diffraction and phased using the two endogenous zinc ions per subunit. The structure reveals a catalytic and cofactor binding domain
Sulfolobus solfataricus
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Zn2+
contains two endogenous zinc ions per subunit.A zinc ion is bound in the loop that protrudes from the catalytic domain. This zinc is tetrahedrally coordinated by residues D94, C97, C100 and C108
Sulfolobus solfataricus
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Sulfolobus solfataricus
Q97YM2
-
-
Sulfolobus solfataricus P2
Q97YM2
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
6-deoxy-L-galactose + NAD+
i.e. L-fucose. The enzyme is specific for sugars with D-arabinose-type hydroxyl group stereo-configurations at C3 and C4. This configuration is shared among the hexoses L-fucose (6-deoxy-L-galactose) and L-galactose, and the pentose D-ribose. Although the highest activity is observed with L-fucose in combination with NAD+, the remaining sugars are oxidized at higher rates using NADP+
681445
Sulfolobus solfataricus
6-deoxy-L-galactono-1,5-lactone + NADH
-
-
-
?
6-deoxy-L-galactose + NAD+
i.e. L-fucose. The enzyme is specific for sugars with D-arabinose-type hydroxyl group stereo-configurations at C3 and C4. This configuration is shared among the hexoses L-fucose (6-deoxy-L-galactose) and L-galactose, and the pentose D-ribose. Although the highest activity is observed with L-fucose in combination with NAD+, the remaining sugars are oxidized at higher rates using NADP+
681445
Sulfolobus solfataricus P2
6-deoxy-L-galactono-1,5-lactone + NADH
-
-
-
?
Subunits
Subunits
Commentary
Organism
homotetramer
-
Sulfolobus solfataricus
Cofactor
Cofactor
Commentary
Organism
Structure
NAD+
the enzyme is specific for sugars with D-arabinose-type hydroxyl group stereo-configurations at C3 and C4. This configuration is shared among the hexoses L-fucose (6-deoxy-L-galactose) and L-galactose, and the pentose D-ribose. Although the highest activity is observed with L-fucose in combination with NAD+, the remaining sugars are oxidized at higher rates using NADP+
Sulfolobus solfataricus
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NAD+
the enzyme is specific for sugars with D-arabinose-type hydroxyl group stereo-configurations at C3 and C4. This configuration is shared among the hexoses L-fucose (6-deoxy-L-galactose) and L-galactose, and the pentose D-ribose. Although the highest activity is observed with L-fucose in combination with NAD+, the remaining sugars are oxidized at higher rates using NADP+
Sulfolobus solfataricus
Crystallization (Commentary) (protein specific)
Crystallization
Organism
the structure is solved to a resolution of 1.80 A by single-wavelength anomalous diffraction and phased using the two endogenous zinc ions per subunit. The structure reveals a catalytic and cofactor binding domain
Sulfolobus solfataricus
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Zn2+
contains two endogenous zinc ions per subunit.A zinc ion is bound in the loop that protrudes from the catalytic domain. This zinc is tetrahedrally coordinated by residues D94, C97, C100 and C108
Sulfolobus solfataricus
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
6-deoxy-L-galactose + NAD+
i.e. L-fucose. The enzyme is specific for sugars with D-arabinose-type hydroxyl group stereo-configurations at C3 and C4. This configuration is shared among the hexoses L-fucose (6-deoxy-L-galactose) and L-galactose, and the pentose D-ribose. Although the highest activity is observed with L-fucose in combination with NAD+, the remaining sugars are oxidized at higher rates using NADP+
681445
Sulfolobus solfataricus
6-deoxy-L-galactono-1,5-lactone + NADH
-
-
-
?
6-deoxy-L-galactose + NAD+
i.e. L-fucose. The enzyme is specific for sugars with D-arabinose-type hydroxyl group stereo-configurations at C3 and C4. This configuration is shared among the hexoses L-fucose (6-deoxy-L-galactose) and L-galactose, and the pentose D-ribose. Although the highest activity is observed with L-fucose in combination with NAD+, the remaining sugars are oxidized at higher rates using NADP+
681445
Sulfolobus solfataricus P2
6-deoxy-L-galactono-1,5-lactone + NADH
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
homotetramer
-
Sulfolobus solfataricus
Other publictions for EC 1.1.1.122
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)
681445
Brouns
Crystal structure and biochemi ...
Sulfolobus solfataricus, Sulfolobus solfataricus P2
J. Mol. Biol.
371
1249-1260
2007
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719837
Brouns
Identification of the missing ...
Sulfolobus solfataricus, Sulfolobus solfataricus P2
J. Biol. Chem.
281
27378-27388
2006
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655086
Bakke
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Improvement in thermal stabili ...
Pseudomonas sp., Pseudomonas sp. No. 1143
Biotechnol. Lett.
24
1075-1078
2002
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285798
Itoh
-
Purification and characterizat ...
Agrobacterium tumefaciens, Agrobacterium tumefaciens K-28
J. Ferment. Bioeng.
77
100-102
1994
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285799
Yamamoto-Otake
Cloning and sequencing of the ...
Pseudomonas sp.
Biosci. Biotechnol. Biochem.
58
2281-2282
1994
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285800
Tsuji
Purification and some properti ...
Agrobacterium tumefaciens
Biochim. Biophys. Acta
1117
167-173
1992
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285801
Guimaraes
-
Purification and general prope ...
Aureobasidium pullulans
Arq. Biol. Tecnol. (Curitiba)
32
575-587
1989
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285802
Sasajima
Oxidation of L-glucose by a ps ...
Paraburkholderia caryophylli
Biochim. Biophys. Acta
571
120-126
1979
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285805
Endo
Isolation and characterization ...
Oryctolagus cuniculus
J. Biochem.
86
1559-1565
1979
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3
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285803
Mobley
The physical properties of NAD ...
Ovis aries aries
Arch. Biochem. Biophys.
186
184-188
1978
5
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285804
Mobley
L-Fucose dehydrogenase from sh ...
Ovis aries aries
Methods Enzymol.
41B
173-177
1975
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6
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285806
Schacter
Isolation of diphosphopyridine ...
Sus scrofa
J. Biol. Chem.
244
4785-4792
1969
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