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Literature summary 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

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

Metals/Ions

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

Organism

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

Purification (Commentary)

EC Number Purification (Comment) Organism
6.3.2.12
-
Escherichia coli

Substrates and Products (Substrate)

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