BRENDA - Enzyme Database show
show all sequences of 1.1.1.173

Eukaryotic and bacterial gene clusters related to an alternative pathway of non-phosphorylated L-rhamnose metabolism

Watanabe, S.; Saimura, M.; Makino, K.; J. Biol. Chem. 283, 20372-20382 (2008)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
gene LRA1, DNA and amino acid sequence determination and analysis, genetic organization, functional expression of His-tagged enzyme in Escherichia coli
Debaryomyces hansenii
gene LRA1, DNA and amino acid sequence determination and analysis, genetic organization, functional expression of His-tagged enzyme in Escherichia coli
Scheffersomyces stipitis
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
1.71
-
L-rhamnose
pH 9.0, 30C, recombinant enzyme
Scheffersomyces stipitis
9.35
-
L-rhamnose
pH 9.0, 30C, recombinant enzyme
Debaryomyces hansenii
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
25000
-
x * 25000, SDS-PAGE
Scheffersomyces stipitis
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
L-rhamnose + NAD+
Debaryomyces hansenii
-
L-rhamno-1,4-lactone + NADH
-
-
r
L-rhamnose + NAD+
Scheffersomyces stipitis
-
L-rhamno-1,4-lactone + NADH
-
-
r
L-rhamnose + NAD+
Debaryomyces hansenii NBRC0083
-
L-rhamno-1,4-lactone + NADH
-
-
r
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Debaryomyces hansenii
-
strain NBRC0083, gene LRA1
-
Debaryomyces hansenii NBRC0083
-
strain NBRC0083, gene LRA1
-
Scheffersomyces stipitis
-
strain CBS 6054, gene LRA1
-
Purification (Commentary)
Commentary
Organism
native enzyme 42.8fold by anion exchange chromatography, ultrafiltration, gel filtration, hydroxyapatite chromatography, and again gel filtration, recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography
Scheffersomyces stipitis
recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography
Debaryomyces hansenii
Reaction
Reaction
Commentary
Organism
L-rhamnofuranose + NAD+ = L-rhamno-1,4-lactone + NADH + H+
the catalytic triad is formed by conserved Ser-Tyr-Lys residues
Debaryomyces hansenii
L-rhamnofuranose + NAD+ = L-rhamno-1,4-lactone + NADH + H+
the catalytic triad is formed by conserved Ser148-Tyr161-Lys165 residues
Scheffersomyces stipitis
Specific Activity [micromol/min/mg]
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
29.9
-
purified native enzyme
Scheffersomyces stipitis
50.4
-
purified recombinant enzyme
Scheffersomyces stipitis
53.3
-
purified recombinant enzyme
Debaryomyces hansenii
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
L-rhamnose + NAD+
-
687737
Debaryomyces hansenii
L-rhamno-1,4-lactone + NADH
-
-
-
r
L-rhamnose + NAD+
-
687737
Scheffersomyces stipitis
L-rhamno-1,4-lactone + NADH
-
-
-
r
L-rhamnose + NAD+
-
687737
Debaryomyces hansenii NBRC0083
L-rhamno-1,4-lactone + NADH
-
-
-
r
Subunits
Subunits
Commentary
Organism
?
x * 25000, SDS-PAGE
Scheffersomyces stipitis
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
30
-
oxidation assay at
Debaryomyces hansenii
30
-
oxidation assay at
Scheffersomyces stipitis
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
1510
-
L-rhamnose
pH 9.0, 30C, recombinant enzyme
Scheffersomyces stipitis
2860
-
L-rhamnose
pH 9.0, 30C, recombinant enzyme
Debaryomyces hansenii
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
9
-
oxidation assay at
Debaryomyces hansenii
9
-
oxidation assay at
Scheffersomyces stipitis
Cofactor
Cofactor
Commentary
Organism
Structure
NAD+
strictly dependent on
Debaryomyces hansenii
NAD+
strictly dependent on
Scheffersomyces stipitis
NADH
strictly dependent on
Debaryomyces hansenii
NADH
strictly dependent on
Scheffersomyces stipitis
Cloned(Commentary) (protein specific)
Commentary
Organism
gene LRA1, DNA and amino acid sequence determination and analysis, genetic organization, functional expression of His-tagged enzyme in Escherichia coli
Debaryomyces hansenii
gene LRA1, DNA and amino acid sequence determination and analysis, genetic organization, functional expression of His-tagged enzyme in Escherichia coli
Scheffersomyces stipitis
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NAD+
strictly dependent on
Debaryomyces hansenii
NAD+
strictly dependent on
Scheffersomyces stipitis
NADH
strictly dependent on
Debaryomyces hansenii
NADH
strictly dependent on
Scheffersomyces stipitis
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
1.71
-
L-rhamnose
pH 9.0, 30C, recombinant enzyme
Scheffersomyces stipitis
9.35
-
L-rhamnose
pH 9.0, 30C, recombinant enzyme
Debaryomyces hansenii
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
25000
-
x * 25000, SDS-PAGE
Scheffersomyces stipitis
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
L-rhamnose + NAD+
Debaryomyces hansenii
-
L-rhamno-1,4-lactone + NADH
-
-
r
L-rhamnose + NAD+
Scheffersomyces stipitis
-
L-rhamno-1,4-lactone + NADH
-
-
r
L-rhamnose + NAD+
Debaryomyces hansenii NBRC0083
-
L-rhamno-1,4-lactone + NADH
-
-
r
Purification (Commentary) (protein specific)
Commentary
Organism
native enzyme 42.8fold by anion exchange chromatography, ultrafiltration, gel filtration, hydroxyapatite chromatography, and again gel filtration, recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography
Scheffersomyces stipitis
recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography
Debaryomyces hansenii
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
29.9
-
purified native enzyme
Scheffersomyces stipitis
50.4
-
purified recombinant enzyme
Scheffersomyces stipitis
53.3
-
purified recombinant enzyme
Debaryomyces hansenii
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
L-rhamnose + NAD+
-
687737
Debaryomyces hansenii
L-rhamno-1,4-lactone + NADH
-
-
-
r
L-rhamnose + NAD+
-
687737
Scheffersomyces stipitis
L-rhamno-1,4-lactone + NADH
-
-
-
r
L-rhamnose + NAD+
-
687737
Debaryomyces hansenii NBRC0083
L-rhamno-1,4-lactone + NADH
-
-
-
r
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 25000, SDS-PAGE
Scheffersomyces stipitis
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
30
-
oxidation assay at
Debaryomyces hansenii
30
-
oxidation assay at
Scheffersomyces stipitis
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
1510
-
L-rhamnose
pH 9.0, 30C, recombinant enzyme
Scheffersomyces stipitis
2860
-
L-rhamnose
pH 9.0, 30C, recombinant enzyme
Debaryomyces hansenii
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
9
-
oxidation assay at
Debaryomyces hansenii
9
-
oxidation assay at
Scheffersomyces stipitis
Other publictions for EC 1.1.1.173
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)
733813
Bae
Identification and characteriz ...
Sulfobacillus thermosulfidooxidans
Extremophiles
19
469-478
2015
-
-
-
-
-
-
-
-
-
-
-
-
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5
-
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4
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5
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1
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1
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2
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2
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4
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5
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1
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1
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-
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-
-
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686697
Koivistoinen
Identification in the yeast Pi ...
Scheffersomyces stipitis, Scheffersomyces stipitis NRC5568
FEBS J.
275
2482-2488
2008
1
-
1
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-
1
4
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1
2
-
6
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-
1
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-
1
-
10
1
1
-
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-
1
-
-
3
-
-
-
1
-
1
3
-
-
-
-
1
-
4
-
-
1
2
-
-
-
1
-
-
1
-
10
1
1
-
-
-
1
-
-
-
-
-
-
-
-
-
687737
Watanabe
Eukaryotic and bacterial gene ...
Debaryomyces hansenii, Debaryomyces hansenii NBRC0083, Scheffersomyces stipitis
J. Biol. Chem.
283
20372-20382
2008
-
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2
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-
2
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-
1
3
-
10
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2
2
-
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3
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3
1
2
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2
2
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4
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2
4
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2
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1
3
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2
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3
-
3
1
2
-
-
2
2
-
-
-
-
-
-
-
-
-
286118
Mostad
The stereospecificity of hydro ...
Aureobasidium pullulans
Biochem. Biophys. Res. Commun.
233
681-686
1997
-
-
-
-
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-
-
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-
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1
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1
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1
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-
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-
-
-
-
-
-
-
-
347736
Twerdochlib
-
L-Rhamnose metabolism in Pichi ...
Scheffersomyces stipitis
Can. J. Microbiol.
40
896-902
1994
-
-
-
-
-
-
-
-
-
-
-
2
-
1
-
-
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-
-
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2
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2
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2
-
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-
-
-
-
-
-
-
-
-
-
-
347735
Pardo
-
Pichia stipitis L-rhamnose deh ...
Scheffersomyces stipitis
Can. J. Microbiol.
38
417-422
1992
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
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-
-
-
1
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1
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-
-
-
-
-
-
347732
Pittner
-
The application of immobilized ...
Aureobasidium pullulans
Appl. Biochem. Biotechnol.
16
15-24
1987
-
-
-
-
-
-
-
2
-
-
-
1
-
1
-
-
-
-
-
-
1
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1
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1
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2
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2
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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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-
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-
-
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347733
Rigo
L-Rhamnose dehydrogenase of pu ...
Aureobasidium pullulans
Biochim. Biophys. Acta
445
286-293
1976
-
-
-
-
-
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6
2
-
-
-
1
-
1
-
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1
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1
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
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1
1
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1
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