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Literature summary for 6.3.2.12 extracted from

  • Ferone, R.; Warskow, A.
    Co-purification of dihydrofolate synthetase and N-10formyltetrahydropteroyldiglutamate synthetase from E. coli (1983), Adv. Exp. Med. Biol., 163, 167-181.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
additional information no inhibition by 10N-formyltetrahydropteroyldiglutamate Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
K+ monovalent cation required Escherichia coli
K+ monovalent cation requirement is satisfied by K+, Rb+ or NH4+ Escherichia coli
NH4+ monovalent cation requirement is satisfied by K+, Rb+ or NH4+ Escherichia coli
Rb+ monovalent cation requirement is satisfied by K+, Rb+ or NH4+ Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
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enzyme posseses dihydrofolate synthetase and N10-formyltetrahydropteroyldiglutamate synthetase activity
-

Purification (Commentary)

Purification (Comment) Organism
-
Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + 7,8-dihydropteroate + L-Glu
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Escherichia coli ADP + phosphate + 7,8-dihydrofolate
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