BRENDA - Enzyme Database show
show all sequences of 1.1.1.48

Physical and kinetic effects on introduction of various linker regions in beta-galactosidase/galactose dehydrogenase fusion enzymes

Carlsson, H.; Ljung, S.; Bulow, L.; Biochim. Biophys. Acta 1293, 154-160 (1996)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
beta-galactosidase-galactose dehydrogenase fusion enzymes, expressed in Escherichia coli
Pseudomonas fluorescens
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.15
-
NAD+
-
Pseudomonas fluorescens
0.23
-
D-galactose
-
Pseudomonas fluorescens
0.25
-
NAD+
beta-galactosidase-galactose dehydrogenase fusion enzymes
Pseudomonas fluorescens
0.37
-
D-galactose
beta-galactosidase-galactose dehydrogenase fusion enzyme, 13 amino acids as linker
Pseudomonas fluorescens
0.4
-
D-galactose
beta-galactosidase-galactose dehydrogenase fusion enzyme, 9 amino acids as linker
Pseudomonas fluorescens
0.45
-
D-galactose
beta-galactosidase-galactose dehydrogenase fusion enzyme, 3 amino acids as linker
Pseudomonas fluorescens
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
D-galactose + NAD+
Pseudomonas fluorescens
-
D-galactono-1,5-lactone + NADH
-
Pseudomonas fluorescens
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Pseudomonas fluorescens
-
-
-
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
17
-
beta-galactosidase-galactose dehydrogenase fusion enzyme, 3 amino acids as linker
Pseudomonas fluorescens
27
-
beta-galactosidase-galactose dehydrogenase fusion enzyme, 13 amino acids as linker
Pseudomonas fluorescens
29
-
beta-galactosidase-galactose dehydrogenase fusion enzyme, 9 amino acids as linker
Pseudomonas fluorescens
34
-
-
Pseudomonas fluorescens
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-galactose + NAD+
-
286955
Pseudomonas fluorescens
D-galactono-1,5-lactone + NADH
-
286955
Pseudomonas fluorescens
?
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
50
-
native enzyme, 70% activity after 20 min, 30% after 60 min, 20% after 90 min, beta-galactosidase-galactose dehydrogenase fusion enzymes, 80% activity after 90 min
Pseudomonas fluorescens
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
9.9
-
-
Pseudomonas fluorescens
Cloned(Commentary) (protein specific)
Commentary
Organism
beta-galactosidase-galactose dehydrogenase fusion enzymes, expressed in Escherichia coli
Pseudomonas fluorescens
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.15
-
NAD+
-
Pseudomonas fluorescens
0.23
-
D-galactose
-
Pseudomonas fluorescens
0.25
-
NAD+
beta-galactosidase-galactose dehydrogenase fusion enzymes
Pseudomonas fluorescens
0.37
-
D-galactose
beta-galactosidase-galactose dehydrogenase fusion enzyme, 13 amino acids as linker
Pseudomonas fluorescens
0.4
-
D-galactose
beta-galactosidase-galactose dehydrogenase fusion enzyme, 9 amino acids as linker
Pseudomonas fluorescens
0.45
-
D-galactose
beta-galactosidase-galactose dehydrogenase fusion enzyme, 3 amino acids as linker
Pseudomonas fluorescens
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
D-galactose + NAD+
Pseudomonas fluorescens
-
D-galactono-1,5-lactone + NADH
-
Pseudomonas fluorescens
?
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
17
-
beta-galactosidase-galactose dehydrogenase fusion enzyme, 3 amino acids as linker
Pseudomonas fluorescens
27
-
beta-galactosidase-galactose dehydrogenase fusion enzyme, 13 amino acids as linker
Pseudomonas fluorescens
29
-
beta-galactosidase-galactose dehydrogenase fusion enzyme, 9 amino acids as linker
Pseudomonas fluorescens
34
-
-
Pseudomonas fluorescens
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-galactose + NAD+
-
286955
Pseudomonas fluorescens
D-galactono-1,5-lactone + NADH
-
286955
Pseudomonas fluorescens
?
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
50
-
native enzyme, 70% activity after 20 min, 30% after 60 min, 20% after 90 min, beta-galactosidase-galactose dehydrogenase fusion enzymes, 80% activity after 90 min
Pseudomonas fluorescens
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
9.9
-
-
Pseudomonas fluorescens
Other publictions for EC 1.1.1.48
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)
655445
Mazitsos
Galactosyl-mimodye ligands for ...
Pseudomonas fluorescens
Eur. J. Biochem.
269
5391-5405
2002
-
1
-
-
-
-
1
-
-
-
-
-
-
3
-
-
1
-
-
1
-
-
1
1
1
-
-
-
1
-
-
2
-
-
-
-
1
-
2
-
-
-
-
1
-
-
-
-
-
-
-
-
-
1
-
1
-
-
1
1
1
-
-
-
1
-
-
-
-
-
-
-
-
-
286955
Carlsson
Physical and kinetic effects o ...
Pseudomonas fluorescens
Biochim. Biophys. Acta
1293
154-160
1996
-
-
1
-
-
-
-
6
-
-
-
1
-
1
-
-
-
-
-
-
4
-
1
-
-
-
1
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
6
-
-
-
1
-
-
-
-
-
-
4
-
1
-
-
-
1
-
1
-
-
-
-
-
-
-
-
-
286956
Carlsson
Use of geneticallly prepared e ...
Pseudomonas fluorescens
Anal. Biochem.
218
278-283
1994
-
1
-
-
-
-
-
12
-
-
-
1
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
12
-
-
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
286957
Wong
The deLey-Doudoroff pathway of ...
Azotobacter vinelandii, Pelomonas saccharophila, Pseudomonas fluorescens, Rhizobium meliloti L5-30
Appl. Environ. Microbiol.
60
2065-2068
1994
-
-
-
-
-
-
-
6
4
-
1
6
-
9
-
-
1
-
-
-
7
-
13
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
6
4
-
1
6
-
-
-
1
-
-
7
-
13
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
286958
Lindbladh
Characterization of a recombin ...
Pseudomonas fluorescens
Eur. J. Biochem.
204
241-247
1992
-
-
1
-
-
-
-
-
-
-
-
1
-
1
-
-
1
-
-
-
1
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
1
-
-
1
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
286959
Ljungcrantz
Construction and characterizat ...
Pseudomonas fluorescens
FEBS Lett.
275
91-94
1990
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
1
-
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
1
-
1
-
-
-
-
-
-
-
-
-
286960
Fiedler
The D-galactose dehydrogenase ...
Pseudomonas fluorescens
Appl. Microbiol. Biotechnol.
33
418-423
1990
-
-
1
-
-
-
-
-
-
-
-
1
-
3
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
5093
Arias
Galactose metabolism in Rhizob ...
Rhizobium meliloti L5-30, Sinorhizobium meliloti, Sinorhizobium meliloti UR23
J. Bacteriol.
167
1092-1094
1986
-
-
-
-
-
-
-
-
-
-
-
5
-
3
-
-
-
-
-
-
8
-
10
-
-
-
-
-
-
-
-
-
-
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-
-
-
-
-
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-
-
-
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-
-
5
-
-
-
-
-
-
8
-
10
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
286962
Fjimura
-
Fluorometric method with galac ...
Pseudomonas fluorescens
Methods Enzymol.
6
288-296
1984
-
1
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
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1
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1
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1
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-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
286963
Maier
D-Galactose dehydrogenase from ...
Pseudomonas fluorescens
Methods Enzymol.
89
176-181
1982
-
-
-
-
-
-
-
-
-
-
-
1
-
2
-
-
-
1
-
-
1
1
1
-
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-
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-
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-
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-
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1
-
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-
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-
1
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
286964
Buckel
Expression of Pseudomonas fluo ...
Pseudomonas fluorescens
Gene
16
149-159
1981
-
-
1
-
-
-
-
-
-
-
-
1
-
5
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
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-
1
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
5089
Kurn
Galactose catabolism in Caulob ...
Caulobacter crescentus AE22, Caulobacter crescentus AE23, Caulobacter crescentus CB13
J. Bacteriol.
135
517-520
1978
-
-
-
-
-
-
-
-
-
-
-
3
-
3
-
-
-
-
-
-
3
-
3
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3
-
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3
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
286966
Brendel
Stereochemistry of the hydroge ...
Pseudomonas fluorescens
Biochim. Biophys. Acta
397
1-4
1975
-
-
-
-
-
-
-
-
-
-
-
1
-
2
-
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1
-
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1
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1
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1
-
-
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-
-
-
-
-
-
-
-
-
-
-
-
286967
Ueberschär
Stereospecificity of hydrogen ...
Pelomonas saccharophila, Pseudomonas fluorescens
Biochim. Biophys. Acta
391
15-18
1975
-
-
-
-
-
-
-
-
-
-
-
2
-
4
-
-
-
2
-
-
-
-
2
-
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2
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-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
286968
Wengenmayer
Subunit structure of D-galacto ...
Pelomonas saccharophila
Biochim. Biophys. Acta
386
590-602
1975
-
-
-
-
-
-
-
-
-
-
1
1
-
2
-
-
-
-
-
-
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-
1
1
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1
1
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-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
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-
286969
Kurz
-
UV-Test mit Galactose Dehydrog ...
Pelomonas saccharophila, Pseudomonas fluorescens
Methods Enzym. Anal. , 3rd Ed. (Bergmeyer, H. U. , ed. )
2
1324-1327
1974
-
2
-
-
-
-
-
-
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2
-
2
1
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2
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2
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1
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2
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286970
Ueberschär
Reaction mechanism of D-galact ...
Pelomonas saccharophila, Pseudomonas fluorescens
Eur. J. Biochem.
48
389-405
1974
-
-
-
-
-
-
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-
2
-
2
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2
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2
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2
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2
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-
-
-
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286971
Blachnitzky
D-galactose dehydrogenase from ...
Pelomonas saccharophila, Pseudomonas fluorescens
Eur. J. Biochem.
47
235-250
1974
-
-
-
-
-
-
-
3
-
-
3
2
-
3
-
-
1
-
-
-
1
1
9
2
-
-
-
1
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
3
-
-
3
2
-
-
-
1
-
-
1
1
9
2
-
-
-
1
1
-
1
-
-
-
-
-
-
-
286972
Wengenmayer
Sulfhydryl group reactivity of ...
Pelomonas saccharophila
Eur. J. Biochem.
43
49-58
1974
-
-
-
-
-
-
2
-
-
-
-
1
-
1
1
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-
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1
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-
-
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-
-
2
-
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-
1
-
1
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-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
286973
Wengenmayer
D-Galactose dehydrogenase from ...
Pelomonas saccharophila
Eur. J. Biochem.
40
49-61
1973
-
-
-
-
-
-
-
2
-
-
2
1
-
2
1
-
1
-
-
-
1
1
5
1
-
-
1
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
2
1
-
1
-
1
-
-
1
1
5
1
-
-
1
1
1
-
-
-
-
-
-
-
-
-
286974
Wengenmayer
Artefakt-Formen der D-Galaktos ...
Pelomonas saccharophila
Hoppe-Seyler's Z. Physiol. Chem.
354
131-135
1973
-
-
-
-
-
-
-
-
-
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1
-
1
1
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1
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1
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1
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1
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285776
Hu
The regulation of some sugar d ...
Pseudomonas sp., Pseudomonas sp. G6
Biochim. Biophys. Acta
93
237-245
1964
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