Literature summary extracted from
Gabrielsen, M.; Beckham, K.S.; Cogdell, R.J.; Byron, O.; Roe, A.J.
FolX from Pseudomonas aeruginosa is octameric in both crystal and solution (2012), FEBS Lett., 586, 1160-1165.
Application
EC Number |
Application |
Comment |
Organism |
---|
5.1.99.7 |
drug development |
the tetrahydrofolate biosynthetic pathway is an established target for important drugs |
Pseudomonas aeruginosa |
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
5.1.99.7 |
gene folX, recombinant expression |
Pseudomonas aeruginosa |
Crystallization (Commentary)
EC Number |
Crystallization (Comment) |
Organism |
---|
5.1.99.7 |
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]
EC Number |
Molecular Weight [Da] |
Molecular Weight Maximum [Da] |
Comment |
Organism |
---|
5.1.99.7 |
141500 |
- |
analytical ultracentrifugation and sedimentation equilibrium data |
Pseudomonas aeruginosa |
Natural Substrates/ Products (Substrates)
EC Number |
Natural Substrates |
Organism |
Comment (Nat. Sub.) |
Natural Products |
Comment (Nat. Pro.) |
Rev. |
Reac. |
---|
5.1.99.7 |
7,8-dihydroneopterin 3'-triphosphate |
Pseudomonas aeruginosa |
- |
7,8-dihydromonapterin 3'-triphosphate |
- |
r |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
5.1.99.7 |
Pseudomonas aeruginosa |
Q9HYG7 |
gene folX |
- |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
5.1.99.7 |
recombinant enzyme |
Pseudomonas aeruginosa |
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
5.1.99.7 |
7,8-dihydroneopterin 3'-triphosphate |
- |
Pseudomonas aeruginosa |
7,8-dihydromonapterin 3'-triphosphate |
- |
r |
|
Subunits
EC Number |
Subunits |
Comment |
Organism |
---|
5.1.99.7 |
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
EC Number |
Synonyms |
Comment |
Organism |
---|
5.1.99.7 |
folX |
- |
Pseudomonas aeruginosa |
General Information
EC Number |
General Information |
Comment |
Organism |
---|
5.1.99.7 |
metabolism |
the epimerase catalyzes one step of the tetrahydrofolate biosynthetic pathway, dihydroneopterin triphosphate is converted to dihydromonapterin triphosphate |
Pseudomonas aeruginosa |
5.1.99.7 |
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 |