BRENDA - Enzyme Database show
show all sequences of 1.1.1.173

Identification in the yeast Pichia stipitis of the first L-rhamnose-1-dehydrogenase gene

Koivistoinen, O.M.; Hilditch, S.; Voutilainen, S.P.; Boer, H.; Penttilae, M.; Richard, P.; FEBS J. 275, 2482-2488 (2008)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
additional information
enzyme transcription in Pichia stipitis is induced during growth on L-rhamnose but not on other carbon sources
Scheffersomyces stipitis
Cloned(Commentary)
Commentary
Organism
gene RHA1, DNA and amino acid sequence determination and analysis, expression in Saccharomyces cereviaie
Scheffersomyces stipitis
Inhibitors
Inhibitors
Commentary
Organism
Structure
additional information
D-glucose suppresses the enzyme
Scheffersomyces stipitis
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
substrate specificity, overview
Scheffersomyces stipitis
1.5
-
L-rhamnose
pH 8.0, 30C, recombinant enzyme
Scheffersomyces stipitis
5
-
L-Lyxose
pH 8.0, 30C, recombinant enzyme
Scheffersomyces stipitis
25
-
L-Mannose
pH 8.0, 30C, recombinant enzyme
Scheffersomyces stipitis
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
30000
-
x * 30000, recombinant enzyme, 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+
Scheffersomyces stipitis
the enzyme is involved in the rhamnose metabolism, overview
L-rhamno-1,4-lactone + NADH
-
-
r
L-rhamnose + NAD+
Scheffersomyces stipitis NRC5568
the enzyme is involved in the rhamnose metabolism, overview
L-rhamno-1,4-lactone + NADH
-
-
r
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Scheffersomyces stipitis
-
strain NRC5568, gene RHA1
-
Scheffersomyces stipitis NRC5568
-
strain NRC5568, gene RHA1
-
Purification (Commentary)
Commentary
Organism
recombinant enzyme in analytical amounts from Saccharomyces cerevisiae by anion exchange chromatography, and native and SDS-PAGE, tagging of the enzyme strongly affects its activity, overview
Scheffersomyces stipitis
Specific Activity [micromol/min/mg]
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
0.6
-
purified recombinant enzyme
Scheffersomyces stipitis
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
L-lyxose + NAD+
-
686697
Scheffersomyces stipitis
? + NADH
-
-
-
?
L-lyxose + NAD+
-
686697
Scheffersomyces stipitis NRC5568
? + NADH
-
-
-
?
L-mannose + NAD+
-
686697
Scheffersomyces stipitis
? + NADH
-
-
-
?
L-mannose + NAD+
-
686697
Scheffersomyces stipitis NRC5568
? + NADH
-
-
-
?
L-rhamnose + NAD+
the enzyme is involved in the rhamnose metabolism, overview
686697
Scheffersomyces stipitis
L-rhamno-1,4-lactone + NADH
-
-
-
r
L-rhamnose + NAD+
the heterologous protein shows the highest activity and affinity with L-rhamnose and a lower activity and affinity with L-mannose and L-lyxose
686697
Scheffersomyces stipitis
L-rhamno-1,4-lactone + NADH
-
-
-
r
L-rhamnose + NAD+
the enzyme is involved in the rhamnose metabolism, overview
686697
Scheffersomyces stipitis NRC5568
L-rhamno-1,4-lactone + NADH
-
-
-
r
L-rhamnose + NAD+
the heterologous protein shows the highest activity and affinity with L-rhamnose and a lower activity and affinity with L-mannose and L-lyxose
686697
Scheffersomyces stipitis NRC5568
L-rhamno-1,4-lactone + NADH
-
-
-
r
additional information
substrate specificity, overview
686697
Scheffersomyces stipitis
?
-
-
-
-
additional information
substrate specificity, overview
686697
Scheffersomyces stipitis NRC5568
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
?
x * 30000, recombinant enzyme, SDS-PAGE
Scheffersomyces stipitis
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
30
-
assay at
Scheffersomyces stipitis
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
-
Scheffersomyces stipitis
Cofactor
Cofactor
Commentary
Organism
Structure
additional information
no activity with NADPH
Scheffersomyces stipitis
NAD+
strictly dependent on
Scheffersomyces stipitis
NADH
strictly dependent on
Scheffersomyces stipitis
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
additional information
enzyme transcription in Pichia stipitis is induced during growth on L-rhamnose but not on other carbon sources
Scheffersomyces stipitis
Cloned(Commentary) (protein specific)
Commentary
Organism
gene RHA1, DNA and amino acid sequence determination and analysis, expression in Saccharomyces cereviaie
Scheffersomyces stipitis
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
additional information
no activity with NADPH
Scheffersomyces stipitis
NAD+
strictly dependent on
Scheffersomyces stipitis
NADH
strictly dependent on
Scheffersomyces stipitis
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
additional information
D-glucose suppresses the enzyme
Scheffersomyces stipitis
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
substrate specificity, overview
Scheffersomyces stipitis
1.5
-
L-rhamnose
pH 8.0, 30C, recombinant enzyme
Scheffersomyces stipitis
5
-
L-Lyxose
pH 8.0, 30C, recombinant enzyme
Scheffersomyces stipitis
25
-
L-Mannose
pH 8.0, 30C, recombinant enzyme
Scheffersomyces stipitis
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
30000
-
x * 30000, recombinant enzyme, 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+
Scheffersomyces stipitis
the enzyme is involved in the rhamnose metabolism, overview
L-rhamno-1,4-lactone + NADH
-
-
r
L-rhamnose + NAD+
Scheffersomyces stipitis NRC5568
the enzyme is involved in the rhamnose metabolism, overview
L-rhamno-1,4-lactone + NADH
-
-
r
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant enzyme in analytical amounts from Saccharomyces cerevisiae by anion exchange chromatography, and native and SDS-PAGE, tagging of the enzyme strongly affects its activity, overview
Scheffersomyces stipitis
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
0.6
-
purified recombinant enzyme
Scheffersomyces stipitis
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
L-lyxose + NAD+
-
686697
Scheffersomyces stipitis
? + NADH
-
-
-
?
L-lyxose + NAD+
-
686697
Scheffersomyces stipitis NRC5568
? + NADH
-
-
-
?
L-mannose + NAD+
-
686697
Scheffersomyces stipitis
? + NADH
-
-
-
?
L-mannose + NAD+
-
686697
Scheffersomyces stipitis NRC5568
? + NADH
-
-
-
?
L-rhamnose + NAD+
the enzyme is involved in the rhamnose metabolism, overview
686697
Scheffersomyces stipitis
L-rhamno-1,4-lactone + NADH
-
-
-
r
L-rhamnose + NAD+
the heterologous protein shows the highest activity and affinity with L-rhamnose and a lower activity and affinity with L-mannose and L-lyxose
686697
Scheffersomyces stipitis
L-rhamno-1,4-lactone + NADH
-
-
-
r
L-rhamnose + NAD+
the enzyme is involved in the rhamnose metabolism, overview
686697
Scheffersomyces stipitis NRC5568
L-rhamno-1,4-lactone + NADH
-
-
-
r
L-rhamnose + NAD+
the heterologous protein shows the highest activity and affinity with L-rhamnose and a lower activity and affinity with L-mannose and L-lyxose
686697
Scheffersomyces stipitis NRC5568
L-rhamno-1,4-lactone + NADH
-
-
-
r
additional information
substrate specificity, overview
686697
Scheffersomyces stipitis
?
-
-
-
-
additional information
substrate specificity, overview
686697
Scheffersomyces stipitis NRC5568
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 30000, recombinant enzyme, SDS-PAGE
Scheffersomyces stipitis
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
30
-
assay at
Scheffersomyces stipitis
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
-
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
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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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-
-
-
-
686697
Koivistoinen
Identification in the yeast Pi ...
Scheffersomyces stipitis, Scheffersomyces stipitis NRC5568
FEBS J.
275
2482-2488
2008
1
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1
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-
1
4
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1
2
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6
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1
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1
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10
1
1
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-
1
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3
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1
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1
3
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1
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4
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1
2
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1
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-
1
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10
1
1
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-
1
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-
-
-
-
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-
687737
Watanabe
Eukaryotic and bacterial gene ...
Debaryomyces hansenii, Debaryomyces hansenii NBRC0083, Scheffersomyces stipitis
J. Biol. Chem.
283
20372-20382
2008
-
-
2
-
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-
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2
-
-
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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-
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2
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-
1
3
-
-
-
2
-
-
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
-
-
-
-
-
-
-
-
2
-
-
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-
-
-
-
-
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-
-
2
-
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-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
347735
Pardo
-
Pichia stipitis L-rhamnose deh ...
Scheffersomyces stipitis
Can. J. Microbiol.
38
417-422
1992
-
-
-
-
-
-
-
-
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-
1
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-
1
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1
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-
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-
347732
Pittner
-
The application of immobilized ...
Aureobasidium pullulans
Appl. Biochem. Biotechnol.
16
15-24
1987
-
-
-
-
-
-
-
2
-
-
-
1
-
1
-
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-
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1
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1
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-
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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
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
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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
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1
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1
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1
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-
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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
-
2
-
-
-
1
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1
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1
1
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1
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