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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.
    View publication on PubMedView publication on EuropePMC

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