BRENDA - Enzyme Database
show all sequences of 5.1.99.7

FolX from Pseudomonas aeruginosa is octameric in both crystal and solution

Gabrielsen, M.; Beckham, K.S.; Cogdell, R.J.; Byron, O.; Roe, A.J.; FEBS Lett. 586, 1160-1165 (2012)

Data extracted from this reference:

Application
Application
Commentary
Organism
drug development
the tetrahydrofolate biosynthetic pathway is an established target for important drugs
Pseudomonas aeruginosa
Cloned(Commentary)
Cloned (Commentary)
Organism
gene folX, recombinant expression
Pseudomonas aeruginosa
Crystallization (Commentary)
Crystallization (Commentary)
Organism
purified recombinant enzyme, vapour diffusion method, mixing of 500 nl of 6 mg/ml protein in 20 mM Tris pH 7.5, 50 mM NaCl, with 500 nl of reservoir solution containing 40% v/v 1,2-propanediol, 100 mM HEPES, pH 7.5, 1 week, at room temperature, X-ray diffraction structure determination and analysis at 3.0 A resolution
Pseudomonas aeruginosa
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
141500
-
analytical ultracentrifugation and sedimentation equilibrium data
Pseudomonas aeruginosa
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
7,8-dihydroneopterin 3'-triphosphate
Pseudomonas aeruginosa
-
7,8-dihydromonapterin 3'-triphosphate
-
-
r
Organism
Organism
UniProt
Commentary
Textmining
Pseudomonas aeruginosa
Q9HYG7
gene folX
-
Purification (Commentary)
Purification (Commentary)
Organism
recombinant enzyme
Pseudomonas aeruginosa
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
7,8-dihydroneopterin 3'-triphosphate
-
733859
Pseudomonas aeruginosa
7,8-dihydromonapterin 3'-triphosphate
-
-
-
r
Subunits
Subunits
Commentary
Organism
octamer
the enzyme protein is an octamer both in the crystal structure, and in solution formed by two tetramers. The monomeric enzyme structure comprises a four-stranded antiparallel sheet, composed of beta1 (residues 10-12 and 16-20), beta2 (residues 33-42), beta3 (residues 98-106) and beta4 (residues 114-121), structure comparisons, overview
Pseudomonas aeruginosa
Synonyms
Synonyms
Commentary
Organism
folX
-
Pseudomonas aeruginosa
Application (protein specific)
Application
Commentary
Organism
drug development
the tetrahydrofolate biosynthetic pathway is an established target for important drugs
Pseudomonas aeruginosa
Cloned(Commentary) (protein specific)
Commentary
Organism
gene folX, recombinant expression
Pseudomonas aeruginosa
Crystallization (Commentary) (protein specific)
Crystallization
Organism
purified recombinant enzyme, vapour diffusion method, mixing of 500 nl of 6 mg/ml protein in 20 mM Tris pH 7.5, 50 mM NaCl, with 500 nl of reservoir solution containing 40% v/v 1,2-propanediol, 100 mM HEPES, pH 7.5, 1 week, at room temperature, X-ray diffraction structure determination and analysis at 3.0 A resolution
Pseudomonas aeruginosa
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
141500
-
analytical ultracentrifugation and sedimentation equilibrium data
Pseudomonas aeruginosa
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
7,8-dihydroneopterin 3'-triphosphate
Pseudomonas aeruginosa
-
7,8-dihydromonapterin 3'-triphosphate
-
-
r
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant enzyme
Pseudomonas aeruginosa
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
7,8-dihydroneopterin 3'-triphosphate
-
733859
Pseudomonas aeruginosa
7,8-dihydromonapterin 3'-triphosphate
-
-
-
r
Subunits (protein specific)
Subunits
Commentary
Organism
octamer
the enzyme protein is an octamer both in the crystal structure, and in solution formed by two tetramers. The monomeric enzyme structure comprises a four-stranded antiparallel sheet, composed of beta1 (residues 10-12 and 16-20), beta2 (residues 33-42), beta3 (residues 98-106) and beta4 (residues 114-121), structure comparisons, overview
Pseudomonas aeruginosa
General Information
General Information
Commentary
Organism
metabolism
the epimerase catalyzes one step of the tetrahydrofolate biosynthetic pathway, dihydroneopterin triphosphate is converted to dihydromonapterin triphosphate
Pseudomonas aeruginosa
additional information
the active site of FolX is predicted to comprise residues from two adjacent subunits, which suggests that the tetramer is essential for the activity of the enzyme. Formation of the octamer may play a role in the stability of enzyme FolX
Pseudomonas aeruginosa
General Information (protein specific)
General Information
Commentary
Organism
metabolism
the epimerase catalyzes one step of the tetrahydrofolate biosynthetic pathway, dihydroneopterin triphosphate is converted to dihydromonapterin triphosphate
Pseudomonas aeruginosa
additional information
the active site of FolX is predicted to comprise residues from two adjacent subunits, which suggests that the tetramer is essential for the activity of the enzyme. Formation of the octamer may play a role in the stability of enzyme FolX
Pseudomonas aeruginosa
Other publictions for EC 5.1.99.7
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
Synonyms
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)
733859
Gabrielsen
FolX from Pseudomonas aerugino ...
Pseudomonas aeruginosa
FEBS Lett.
586
1160-1165
2012
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1
1
1
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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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1
1
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2
2
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704330
Pribat
FolX and FolM are essential fo ...
Escherichia coli, Pseudomonas aeruginosa
J. Bacteriol.
192
475-482
2010
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2
-
2
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2
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4
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2
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2
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2
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2
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2
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2
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3
3
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5109
HauŻmann
Biosynthesis of pteridines in ...
Escherichia coli, Escherichia coli XL1-Blue
J. Biol. Chem.
273
17418-17424
1998
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1
-
1
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1
4
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1
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7
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1
1
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1
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3
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1
1
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1
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1
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1
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4
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1
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1
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1
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3
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1
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1
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2
2
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734122
Ahn
Purification, cloning, and fun ...
Escherichia coli
J. Biol. Chem.
272
15323-15328
1997
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1
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3
1
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2
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1
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1
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1
1
1
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1
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1
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3
1
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1
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1
1
1
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1
1
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