BRENDA - Enzyme Database
show all sequences of 1.1.1.292

The structure of substrate-free 1,5-anhydro-D-fructose reductase from Sinorhizobium meliloti 1021 reveals an open enzyme conformation

Schu, M.; Faust, A.; Stosik, B.; Kohring, G.W.; Giffhorn, F.; Scheidig, A.J.; Acta Crystallogr. Sect. F 69, 844-849 (2013)

Data extracted from this reference:

Cloned(Commentary)
Cloned (Commentary)
Organism
expresssion in Escherichia coli
Sinorhizobium meliloti
Crystallization (Commentary)
Crystallization (Commentary)
Organism
in complex with NADP(H), to 1.93 A resolution. The structure displays an empty substrate-binding, showing an open conformation of the enzyme state shortly after the release of product, presumably with bound oxidized cofactor NADP+. Amino-acid residues Lys94, His151, Trp162, Arg163, Asp176 and His180 are involved in substrate binding, catalysis or product release. The side chain of Lys94 may function as a molecular switch
Sinorhizobium meliloti
Organism
Organism
UniProt
Commentary
Textmining
Sinorhizobium meliloti
Q92KZ3
-
-
Cloned(Commentary) (protein specific)
Commentary
Organism
expresssion in Escherichia coli
Sinorhizobium meliloti
Crystallization (Commentary) (protein specific)
Crystallization
Organism
in complex with NADP(H), to 1.93 A resolution. The structure displays an empty substrate-binding, showing an open conformation of the enzyme state shortly after the release of product, presumably with bound oxidized cofactor NADP+. Amino-acid residues Lys94, His151, Trp162, Arg163, Asp176 and His180 are involved in substrate binding, catalysis or product release. The side chain of Lys94 may function as a molecular switch
Sinorhizobium meliloti
Other publictions for EC 1.1.1.292
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
Synonyms
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)
739808
Schu
The structure of substrate-fre ...
Sinorhizobium meliloti
Acta Crystallogr. Sect. F
69
844-849
2013
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685692
Sakuma
Mouse AKR1E1 is an ortholog of ...
Mus musculus, Mus musculus C57/BL6J
Biosci. Biotechnol. Biochem.
72
872-876
2008
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1
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1
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2
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2
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10
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1
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1
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10
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1
1
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667264
Kuehn
Catabolism of 1,5-anhydro-D-fr ...
Ensifer adhaerens, Ensifer adhaerens S-30.7.5
Appl. Environ. Microbiol.
72
1248-1257
2006
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1
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3
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3
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2
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1
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1
11
1
2
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3
1
1
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1
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2
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3
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3
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2
1
11
1
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3
1
1
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1
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667698
Dambe
Crystal structure of NADP(H)-d ...
Ensifer adhaerens
Biochemistry
45
10030-10042
2006
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1
1
9
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21
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1
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1
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13
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1
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1
9
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21
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2
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13
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