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Literature summary for 2.1.2.1 extracted from

  • Stover, P.; Schirch, V.
    5-Formyltetrahydrofolate polyglutamates are slow tight binding inhibitors of serine hydroxymethyltransferase (1991), J. Biol. Chem., 266, 1543-1550.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
5-formyltetrahydrofolate monoglutamate
-
Escherichia coli
5-formyltetrahydrofolate monoglutamate
-
Oryctolagus cuniculus
5-methyltetrahydrofolate monoglutamate
-
Escherichia coli
5-methyltetrahydrofolate monoglutamate
-
Oryctolagus cuniculus
5-Methyltetrahydrofolate triglutamate
-
Escherichia coli
5-Methyltetrahydrofolate triglutamate
-
Oryctolagus cuniculus
additional information
-
Escherichia coli
additional information inhibition kinetics Oryctolagus cuniculus

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasm
-
Escherichia coli 5737
-
cytoplasm
-
Oryctolagus cuniculus 5737
-

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
Oryctolagus cuniculus
-
-
-

Reaction

Reaction Comment Organism Reaction ID
5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine mechanism Escherichia coli
5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine mechanism Oryctolagus cuniculus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-serine + tetrahydrofolate
-
Escherichia coli glycine + 5,10-methylenetetrahydrofolate + H2O
-
?
L-serine + tetrahydrofolate
-
Oryctolagus cuniculus glycine + 5,10-methylenetetrahydrofolate + H2O
-
?

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate
-
Escherichia coli
pyridoxal 5'-phosphate
-
Oryctolagus cuniculus

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
additional information
-
additional information
-
Oryctolagus cuniculus