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Literature summary extracted from

  • Slavik, K.; Zizkovsky, V.; Slavikova, V.; Fort, P.
    The purification of formiminotransferase and cyclodeaminase by combination of affinity chromatography and isoelectric focusing (1974), Biochem. Biophys. Res. Commun., 59, 1173-1184.
    View publication on PubMed

General Stability

EC Number General Stability Organism
2.1.2.5 formiminoglutamate prevents inactivation of enzyme Sus scrofa

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.3.1.4 5-formiminotetrahydrofolate Sus scrofa
-
?
-
?

Organism

EC Number Organism UniProt Comment Textmining
2.1.2.5 Sus scrofa
-
-
-
4.3.1.4 Sus scrofa
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.1.2.5 purification of twin enzyme EC 2.1.2.5 and formiminotetrahydrofolate cyclodeaminase EC 4.3.1.4, combination of affinity chromatography and isoelectric focusing Sus scrofa
4.3.1.4 partial Sus scrofa

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.1.2.5 liver
-
Sus scrofa
-
4.3.1.4 liver
-
Sus scrofa
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
4.3.1.4 additional information
-
-
Sus scrofa

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.2.5 additional information twin enzyme EC 2.1.2.5 and formiminotetrahydrofolate cyclodeaminase EC 4.3.1.4: enzyme system forming N5,10-methenyltetrahydrofolate from formiminoglutamate and tetrahydrofolate Sus scrofa ?
-
?
2.1.2.5 tetrahydrofolate + N-formimino-L-glutamate
-
Sus scrofa 5-formiminotetrahydrofolate + L-glutamate
-
?
4.3.1.4 5-formiminotetrahydrofolate
-
Sus scrofa 5,10-methenyltetrahydrofolate + NH3
-
?
4.3.1.4 5-formiminotetrahydrofolate
-
Sus scrofa ?
-
?

Cofactor

EC Number Cofactor Comment Organism Structure
2.1.2.5 tetrahydrofolate
-
Sus scrofa