Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 6.3.2.17 extracted from

  • Mathieu, M.; Debousker, G.; Vincent, S.; Viviani, F.; Bamas-Jacques, N.; Mikol, V.
    Escherichia coli FolC structure reveals an unexpected dihydrofolate binding site providing an attractive target for anti-microbial therapy (2005), J. Biol. Chem., 280, 18916-18922.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
the folC gene from Escherichia coli is cloned into plasmid pET29. The resulting plasmid, pVRC1432, is transferred into the Escherichia coli BL21 strain Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging drop method in 1.2-1.7 M ammonium sulfate Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
additional information in Escherichia coli, the addition of L-glutamate to dihydropteroate (dihydrofolate synthetase activity) and the subsequent additions of L-glutamate to tetrahydrofolate (folylpolyglutamate synthetase (FPGS) activity) are catalyzed by the same enzyme, FolC. The presence of a folate binding site in Escherichia coli FolC, which is different from the one seen in folylpolyglutamate synthetases, provides avenues for the design of specific inhibitors of this enzyme in antimicrobial therapy Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Synonyms

Synonyms Comment Organism
FolC
-
Escherichia coli