BRENDA - Enzyme Database show
show all sequences of 1.1.1.77

Inactivation of propanediol oxidoreductase of Escherichia coli by metal-catalyzed oxidation

Cabiscol, E.; Badia, J.; Baldoma, L.; Hidalgo, E.; Aguilar, J.; Ros, J.; Biochim. Biophys. Acta 1118, 155-160 (1992)

Data extracted from this reference:

Inhibitors
Inhibitors
Commentary
Organism
Structure
ascorbate
0.025 mM FeCl3 and 0.035 mM ascorbate causes a 90% enzyme inactivation after 120 min = inactivation of metal-catalyzed oxidation; several amino-acids prevent the inactivation; under aerobic conditions 0.025 mM FeCl3 causes a 50% enzyme inactivation after 120 min
Escherichia coli
Fe2+
under anaerobic conditions 0.01 mM Fe2+ and 0.1 mM H2O2 had the effect of 85% enzyme inactivation after 2 min, with addition of 0.0001 mM catalase the inactivation is only 25% after 2 min and with addition of 0.01 mM superoxide dismutase instead of catalse the inactivation is again 82% after 2 min
Escherichia coli
Fe3+
0.025 mM FeCl3 and 0.035 mM ascorbate causes a 90% enzyme inactivation after 120 min = inactivation of metal-catalyzed oxidation; several amino-acids prevent the inactivation; under aerobic conditions 0.025 mM FeCl3 causes a 50% enzyme inactivation after 120 min
Escherichia coli
H2O2
under anaerobic conditions 0.01 mM Fe2+ and 0.1 mM H2O2 had the effect of 85% enzyme inactivation after 2 min, with addition of 0.0001 mM catalase the inactivation is only 25% after 2 min and with addition of 0.01 mM superoxide dismutase instead of catalse the inactivation is again 82% after 2 min
Escherichia coli
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Escherichia coli
-
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(R)-propane-1,2-diol + NAD+
-
287317
Escherichia coli
(R)-lactaldehyde + NADH
-
-
-
?
Cofactor
Cofactor
Commentary
Organism
Structure
NAD+
-
Escherichia coli
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NAD+
-
Escherichia coli
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
ascorbate
0.025 mM FeCl3 and 0.035 mM ascorbate causes a 90% enzyme inactivation after 120 min = inactivation of metal-catalyzed oxidation; several amino-acids prevent the inactivation; under aerobic conditions 0.025 mM FeCl3 causes a 50% enzyme inactivation after 120 min
Escherichia coli
Fe2+
under anaerobic conditions 0.01 mM Fe2+ and 0.1 mM H2O2 had the effect of 85% enzyme inactivation after 2 min, with addition of 0.0001 mM catalase the inactivation is only 25% after 2 min and with addition of 0.01 mM superoxide dismutase instead of catalse the inactivation is again 82% after 2 min
Escherichia coli
Fe3+
0.025 mM FeCl3 and 0.035 mM ascorbate causes a 90% enzyme inactivation after 120 min = inactivation of metal-catalyzed oxidation; several amino-acids prevent the inactivation; under aerobic conditions 0.025 mM FeCl3 causes a 50% enzyme inactivation after 120 min
Escherichia coli
H2O2
under anaerobic conditions 0.01 mM Fe2+ and 0.1 mM H2O2 had the effect of 85% enzyme inactivation after 2 min, with addition of 0.0001 mM catalase the inactivation is only 25% after 2 min and with addition of 0.01 mM superoxide dismutase instead of catalse the inactivation is again 82% after 2 min
Escherichia coli
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(R)-propane-1,2-diol + NAD+
-
287317
Escherichia coli
(R)-lactaldehyde + NADH
-
-
-
?
Other publictions for EC 1.1.1.77
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)
701174
Patel
Rhamnose catabolism in Bactero ...
Bacteroides thetaiotaomicron, Bacteroides thetaiotaomicron VPI-5482
Res. Microbiol.
159
678-684
2008
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1
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1
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2
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5
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2
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2
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2
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-
287317
Cabiscol
Inactivation of propanediol ox ...
Escherichia coli
Biochim. Biophys. Acta
1118
155-160
1992
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4
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2
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1
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1
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4
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1
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137611
Tran-Din
-
Formation of D(-)-1,2-propaned ...
Clostridium sphenoides
Arch. Microbiol.
142
87-92
1985
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1
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1
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2
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1
1
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287310
Weimer
Fermentation of 6-deoxyhexoses ...
Paenibacillus macerans
Appl. Environ. Microbiol.
47
263-267
1984
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1
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3
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1
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287316
Boronat
Metabolism of L-fucose and L-r ...
Escherichia coli
J. Bacteriol.
147
181-185
1981
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2
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2
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1
1
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287309
Kawagishi
Purification of NAD-dependent ...
Microcyclus eburneus
Agric. Biol. Chem.
44
949-950
1980
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287312
Boronat
Rhamnose-induced propanediol o ...
Escherichia coli
J. Bacteriol.
140
320-326
1979
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1
2
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2
1
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2
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1
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7
1
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2
2
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2
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2
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1
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2
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2
1
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1
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7
1
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2
2
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287314
Hacking
Evolution of propanediol utili ...
Escherichia coli
J. Bacteriol.
136
522-530
1978
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-
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1
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2
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287313
Hacking
Disruption of the fucose pathw ...
Escherichia coli
J. Bacteriol.
126
1166-1172
1976
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2
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2
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287315
Cocks
Evolution of L-1,2-propanediol ...
Escherichia coli
J. Bacteriol.
118
83-88
1974
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1
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287308
Ting
The metabolism of lactaldehyde ...
Rattus norvegicus
Biochim. Biophys. Acta
89
217-225
1965
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3
4
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6
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6
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