BRENDA - Enzyme Database show
show all sequences of 3.5.1.22

Pantothenase from Pseudomonas fluorescens

Kalvero Airas, R.; Methods Enzymol. 62, 267-275 (1979)

Data extracted from this reference:

Inhibitors
Inhibitors
Commentary
Organism
Structure
oxalate
-
Pseudomonas fluorescens
oxaloacetate
noncompetitive inhibition, dependent on pH
Pseudomonas fluorescens
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
7.6
-
pantothenic acid
pH-independent theoretical Km
Pseudomonas fluorescens
15
-
pantothenic acid
dependent on pH, phosphate buffer, pH 7.0, 20°C
Pseudomonas fluorescens
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
intracellular
-
Pseudomonas fluorescens
5622
-
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
50000
-
2 * 50000, SDS-PAGE
Pseudomonas fluorescens
97400
-
gel filtration
Pseudomonas fluorescens
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
pantothenic acid + H2O
Pseudomonas fluorescens
sole source of carbon and nitrogen
?
-
-
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Pseudomonas fluorescens
-
-
-
Purification (Commentary)
Commentary
Organism
-
Pseudomonas fluorescens
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
14.8
-
-
Pseudomonas fluorescens
Storage Stability
Storage Stability
Organism
-20°C 20 mM potassium phosphate pH 7, enzyme is made accessible to substrates by freezing and thawing four times, decrease of activity 20% per round of freezing and thawing, frozen enzyme retains activity for at least 2 years
Pseudomonas fluorescens
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
pantothenate + H2O
-
171976
Pseudomonas fluorescens
2,4-dihydroxy-3,3-dimethylbutyric acid + beta-alanine
-
-
-
?
pantothenic acid + H2O
-
171976
Pseudomonas fluorescens
beta-alanine + D-pantoyl lactone
-
-
-
r
pantothenic acid + H2O
-
171976
Pseudomonas fluorescens
beta-alanine + D-pantoic acid
-
171976
Pseudomonas fluorescens
ir
pantothenic acid + H2O
sole source of carbon and nitrogen
171976
Pseudomonas fluorescens
?
-
-
-
-
pantoyl-gamma-aminobutyrate + H2O
-
171976
Pseudomonas fluorescens
4-aminobutyrate + D-pantoate
-
-
-
?
Subunits
Subunits
Commentary
Organism
dimer
2 * 50000, SDS-PAGE
Pseudomonas fluorescens
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
20
-
-
Pseudomonas fluorescens
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
30
35
above 30°C rapidly inactivated, at 35°C inactivation rate 7.2%/min
Pseudomonas fluorescens
pH Range
pH Minimum
pH Maximum
Commentary
Organism
5.5
9.5
-
Pseudomonas fluorescens
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
oxalate
-
Pseudomonas fluorescens
oxaloacetate
noncompetitive inhibition, dependent on pH
Pseudomonas fluorescens
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
7.6
-
pantothenic acid
pH-independent theoretical Km
Pseudomonas fluorescens
15
-
pantothenic acid
dependent on pH, phosphate buffer, pH 7.0, 20°C
Pseudomonas fluorescens
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
intracellular
-
Pseudomonas fluorescens
5622
-
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
50000
-
2 * 50000, SDS-PAGE
Pseudomonas fluorescens
97400
-
gel filtration
Pseudomonas fluorescens
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
pantothenic acid + H2O
Pseudomonas fluorescens
sole source of carbon and nitrogen
?
-
-
-
Purification (Commentary) (protein specific)
Commentary
Organism
-
Pseudomonas fluorescens
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
14.8
-
-
Pseudomonas fluorescens
Storage Stability (protein specific)
Storage Stability
Organism
-20°C 20 mM potassium phosphate pH 7, enzyme is made accessible to substrates by freezing and thawing four times, decrease of activity 20% per round of freezing and thawing, frozen enzyme retains activity for at least 2 years
Pseudomonas fluorescens
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
pantothenate + H2O
-
171976
Pseudomonas fluorescens
2,4-dihydroxy-3,3-dimethylbutyric acid + beta-alanine
-
-
-
?
pantothenic acid + H2O
-
171976
Pseudomonas fluorescens
beta-alanine + D-pantoyl lactone
-
-
-
r
pantothenic acid + H2O
-
171976
Pseudomonas fluorescens
beta-alanine + D-pantoic acid
-
171976
Pseudomonas fluorescens
ir
pantothenic acid + H2O
sole source of carbon and nitrogen
171976
Pseudomonas fluorescens
?
-
-
-
-
pantoyl-gamma-aminobutyrate + H2O
-
171976
Pseudomonas fluorescens
4-aminobutyrate + D-pantoate
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
dimer
2 * 50000, SDS-PAGE
Pseudomonas fluorescens
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
20
-
-
Pseudomonas fluorescens
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
30
35
above 30°C rapidly inactivated, at 35°C inactivation rate 7.2%/min
Pseudomonas fluorescens
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
5.5
9.5
-
Pseudomonas fluorescens
Other publictions for EC 3.5.1.22
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)
171985
Kalvero Airas
Pantothenases from pseudomonad ...
Pseudomonas fluorescens, Pseudomonas fluorescens PS-21
Biochem. J.
250
447-451
1988
-
-
-
-
-
-
8
1
-
-
2
-
-
3
-
-
1
-
-
-
1
-
2
1
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
8
-
1
-
-
2
-
-
-
-
1
-
-
1
-
2
1
1
-
-
-
1
-
-
-
-
-
-
-
-
-
171974
Kalvero Airas
Pantothenase-based assay of pa ...
Pseudomonas fluorescens
Methods Enzymol.
122
33-35
1986
-
1
-
-
-
-
4
1
-
-
-
1
-
1
-
-
1
-
-
-
-
1
2
-
1
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
4
-
1
-
-
-
1
-
-
-
1
-
-
-
1
2
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
171975
Kalvero Airas
Pantothenase-based assay of pa ...
Pseudomonas fluorescens
Anal. Biochem.
134
122-125
1983
-
-
-
-
-
-
7
-
-
-
-
1
-
1
-
-
1
-
-
-
-
1
2
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
7
-
-
-
-
-
1
-
-
-
1
-
-
-
1
2
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
171976
Kalvero Airas
Pantothenase from Pseudomonas ...
Pseudomonas fluorescens
Methods Enzymol.
62
267-275
1979
-
-
-
-
-
-
2
2
1
-
2
1
-
1
-
-
1
-
-
-
1
1
5
1
1
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
2
1
-
2
1
-
-
-
1
-
-
1
1
5
1
1
-
1
-
-
1
-
-
-
-
-
-
-
-
171977
Solberg
Microbiological assay of panto ...
Lactobacillus plantarum, Pediococcus acidilactici
Methods Enzymol.
62
201-205
1979
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
171978
Kalvero Airas
Kinetic study on the reaction ...
Pseudomonas fluorescens
Biochemistry
17
4932-4939
1978
-
-
-
-
-
-
2
1
-
-
-
1
-
1
-
-
1
-
-
-
1
-
2
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
1
-
-
-
1
-
-
-
1
-
-
1
-
2
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
171979
Kalvero Airas
On the partial reactivation of ...
Pseudomonas fluorescens
Biochim. Biophys. Acta
452
201-208
1976
-
-
-
-
-
-
7
-
-
-
-
1
-
2
-
-
1
-
-
-
-
2
2
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
7
-
-
-
-
-
1
-
-
-
1
-
-
-
2
2
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
171980
Kalvero Airas
Thermal inactivation of pantot ...
Pseudomonas fluorescens
Biochim. Biophys. Acta
452
193-200
1976
-
-
-
-
-
-
2
-
-
-
-
1
-
2
-
-
1
-
-
-
-
1
2
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
1
-
-
-
1
-
-
-
1
2
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
171981
Kalvero Airas
Kinetic studies on pantothenas ...
Pseudomonas fluorescens, Pseudomonas fluorescens P-2
Biochem. J.
157
415-421
1976
-
-
-
-
-
-
4
8
-
-
-
2
-
6
-
-
1
-
-
-
-
-
4
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
4
-
8
-
-
-
2
-
-
-
1
-
-
-
-
4
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
171982
Kalvero Airas
Purification and properties of ...
Pseudomonas fluorescens, Pseudomonas fluorescens P-2
Biochem. J.
157
409-413
1976
-
-
-
-
-
-
-
-
-
-
3
2
-
7
-
-
1
-
-
-
2
3
4
1
-
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
3
2
-
-
-
1
-
-
2
3
4
1
-
-
1
-
-
-
1
-
-
-
-
-
-
-
171983
Kalvero Airas
Thermal inactivation and react ...
Pseudomonas fluorescens
Biochem. J.
130
111-119
1972
-
-
-
-
-
-
4
-
-
-
-
1
-
3
-
-
-
-
-
-
-
-
2
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
4
-
-
-
-
-
1
-
-
-
-
-
-
-
-
2
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
171984
Nurmikko
The bacterial degradation of p ...
Pseudomonas fluorescens, Pseudomonas fluorescens P-2
Biochemistry
5
399-403
1966
-
-
-
-
-
-
3
1
-
-
-
2
-
5
-
-
1
-
-
-
-
-
4
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
3
-
1
-
-
-
2
-
-
-
1
-
-
-
-
4
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-