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Literature summary extracted from

  • Akhtar, M.; El-Obeid, H.A.
    Interaction of serine transhydroxymethylase and threonine aldolase activities (1972), Biochim. Biophys. Acta, 791, 791-799.
No PubMed abstract available

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.1.2.1 Bromopyruvate irreversible inactivation, substrates partially protect Oryctolagus cuniculus
2.1.2.1 Chloroacetaldehyde irreversible inactivation, substrates partially protect Oryctolagus cuniculus
2.1.2.1 iodoacetamide irreversible inactivation, substrates partially protect Oryctolagus cuniculus
2.1.2.1 additional information not: chloroacetamide; not: iodoacetate Oryctolagus cuniculus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.1.2.1 cytoplasm
-
 Oryctolagus cuniculus 5737
-

Organism

EC Number Organism UniProt Comment Textmining
2.1.2.1 Oryctolagus cuniculus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.1.2.1
-
 Oryctolagus cuniculus

Reaction

EC Number Reaction Comment Organism Reaction ID
2.1.2.1 5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine mechanism Oryctolagus cuniculus
a

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.1.2.1 additional information
-
-
 Oryctolagus cuniculus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.2.1 L-serine + tetrahydrofolate
-
 Oryctolagus cuniculus glycine + 5,10-methylenetetrahydrofolate + H2O
-
 r

Cofactor

EC Number Cofactor Comment Organism Structure
2.1.2.1 pyridoxal 5'-phosphate
-
 Oryctolagus cuniculus