BRENDA - Enzyme Database show
show all sequences of 1.1.1.106

Evidence for the importance of cysteine and arginine residues in Pseudomonas fluorescens UK-1 pantoate dehydrogenase

Myöhänen, T.; Mäntsälä, P.; Biochim. Biophys. Acta 614, 266-273 (1980)

Data extracted from this reference:

General Stability
General Stability
Organism
unstable without 2-mercaptoethanol, NAD+ stabilizes to a certain extent, the enzyme is unstable below pH 5.5 and above pH 10.0 even in the presence of NAD+
Pseudomonas fluorescens
Inhibitors
Inhibitors
Commentary
Organism
Structure
5,5'-dithiobis(2-nitrobenzoic acid)
1 mM, 50% inhibition after 4.6 min, half-inactivation time increases to 7.0 min in the presence of 20 mM D-pantoate
Pseudomonas fluorescens
iodacetic acid
1 mM, 50% inhibition after 14 min, half-inactivation time increases to 29.0 min in the presence of 20 mM D-pantoate, 70% inhibition within 50 min at pH 7.2, 20 mM pantoate decreases inactivation from 70 to 30%
Pseudomonas fluorescens
p-chloromercuribenzoate
0.1 mM, 85% inhibition after 15 min, 200 mM 2-mercaptoethanol restores 70% of enzyme activity within 10 min, 20 mM D-pantoate and 1 mM NAD+ prevent inactivation when added simultaneously
Pseudomonas fluorescens
Phenylglyoxal
5.3 mM, 70% inhibition in borate buffer, 92% inhibition in NaHCO3 buffer within 10 min, complete inactivation after prolonged incubation with phenylglyoxal, NAD+ and D-pantoate increase half-inactivation time from 6 min without substrates to 40 and 17 min respectively
Pseudomonas fluorescens
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.078
-
NAD+
-
Pseudomonas fluorescens
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
(R)-pantoate + NAD+
Pseudomonas fluorescens
-
(R)-4-dehydropantoate + NADH
-
Pseudomonas fluorescens
?
(R)-pantoate + NAD+
Pseudomonas fluorescens UK1
-
(R)-4-dehydropantoate + NADH
-
Pseudomonas fluorescens UK1
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Pseudomonas fluorescens
-
UK1
-
Pseudomonas fluorescens UK1
-
UK1
-
Purification (Commentary)
Commentary
Organism
ammonium sulfate, 5'-AMP-Sepharose 4B
Pseudomonas fluorescens
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(R)-pantoate + NAD+
-
285729
Pseudomonas fluorescens
(R)-4-dehydropantoate + NADH
-
285729
Pseudomonas fluorescens
?
(R)-pantoate + NAD+
-
285729
Pseudomonas fluorescens UK1
(R)-4-dehydropantoate + NADH
-
285729
Pseudomonas fluorescens UK1
?
Cofactor
Cofactor
Commentary
Organism
Structure
NAD+
-
Pseudomonas fluorescens
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NAD+
-
Pseudomonas fluorescens
General Stability (protein specific)
General Stability
Organism
unstable without 2-mercaptoethanol, NAD+ stabilizes to a certain extent, the enzyme is unstable below pH 5.5 and above pH 10.0 even in the presence of NAD+
Pseudomonas fluorescens
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
5,5'-dithiobis(2-nitrobenzoic acid)
1 mM, 50% inhibition after 4.6 min, half-inactivation time increases to 7.0 min in the presence of 20 mM D-pantoate
Pseudomonas fluorescens
iodacetic acid
1 mM, 50% inhibition after 14 min, half-inactivation time increases to 29.0 min in the presence of 20 mM D-pantoate, 70% inhibition within 50 min at pH 7.2, 20 mM pantoate decreases inactivation from 70 to 30%
Pseudomonas fluorescens
p-chloromercuribenzoate
0.1 mM, 85% inhibition after 15 min, 200 mM 2-mercaptoethanol restores 70% of enzyme activity within 10 min, 20 mM D-pantoate and 1 mM NAD+ prevent inactivation when added simultaneously
Pseudomonas fluorescens
Phenylglyoxal
5.3 mM, 70% inhibition in borate buffer, 92% inhibition in NaHCO3 buffer within 10 min, complete inactivation after prolonged incubation with phenylglyoxal, NAD+ and D-pantoate increase half-inactivation time from 6 min without substrates to 40 and 17 min respectively
Pseudomonas fluorescens
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.078
-
NAD+
-
Pseudomonas fluorescens
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
(R)-pantoate + NAD+
Pseudomonas fluorescens
-
(R)-4-dehydropantoate + NADH
-
Pseudomonas fluorescens
?
(R)-pantoate + NAD+
Pseudomonas fluorescens UK1
-
(R)-4-dehydropantoate + NADH
-
Pseudomonas fluorescens UK1
?
Purification (Commentary) (protein specific)
Commentary
Organism
ammonium sulfate, 5'-AMP-Sepharose 4B
Pseudomonas fluorescens
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(R)-pantoate + NAD+
-
285729
Pseudomonas fluorescens
(R)-4-dehydropantoate + NADH
-
285729
Pseudomonas fluorescens
?
(R)-pantoate + NAD+
-
285729
Pseudomonas fluorescens UK1
(R)-4-dehydropantoate + NADH
-
285729
Pseudomonas fluorescens UK1
?
Other publictions for EC 1.1.1.106
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)
285729
Myöhänen
Evidence for the importance of ...
Pseudomonas fluorescens, Pseudomonas fluorescens UK1
Biochim. Biophys. Acta
614
266-273
1980
-
-
-
-
-
1
4
1
-
-
-
2
-
4
-
-
1
-
-
-
-
-
2
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
1
-
4
-
1
-
-
-
2
-
-
-
1
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
207979
Mäntsälä
Purification of pantoate and d ...
Pseudomonas fluorescens, Pseudomonas fluorescens UK1
Biochim. Biophys. Acta
526
25-33
1978
-
-
-
-
-
-
-
-
-
-
3
2
-
4
-
-
1
-
-
-
1
-
2
1
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
3
2
-
-
-
1
-
-
1
-
2
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
285731
Goodhue
The bacterial degradation of p ...
Pseudomonas sp. P2
Biochemistry
5
403-408
1966
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-
-
-
-
-
-
2
-
-
-
1
-
1
-
-
1
-
-
-
1
1
2
-
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-
-
1
-
1
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-
1
-
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2
-
-
-
1
-
-
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1
-
-
1
1
2
-
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1
-
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-