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Literature summary extracted from

  • Paquin, J.; Baugh, C.M.; MacKenzie, R.E.
    Channeling between the active sites of formiminotransferase-cyclodeaminase. Binding and kinetic studies (1985), J. Biol. Chem., 260, 14925-14931.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.3.1.4 (6S)-5,6,7,8-tetrahydropteroylpolyglutamate
-
Sus scrofa

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.3.1.4 0.0012
-
(6S)-5-formimino-5,6,7,8-tetrahydropteroylhexaglutamate
-
Sus scrofa
4.3.1.4 0.002
-
(6S)-5-formimino-5,6,7,8-tetrahydropteroylpentaglutamate
-
Sus scrofa
4.3.1.4 0.0021
-
(6S)-5-formimino-5,6,7,8-tetrahydropteroylheptaglutamate
-
Sus scrofa
4.3.1.4 0.0029
-
(6S)-5-formimino-5,6,7,8-tetrahydropteroyltetraglutamate
-
Sus scrofa
4.3.1.4 0.021
-
(6S)-5-formimino-5,6,7,8-tetrahydropteroyltriglutamate
-
Sus scrofa
4.3.1.4 0.149
-
(6S)-5-formimino-5,6,7,8-tetrahydropteroylglutamate
-
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
-
?
-
?
4.3.1.4 additional information Sus scrofa folate-dependent bifunctional enzyme formiminoglutamate: tetrahydrofolate formiminotransferase-formiminotetrahydrofolate cyclodeaminase catalyzes two sequential reactions of the histidine degradation pathway ?
-
?
4.3.1.4 additional information Sus scrofa direct transfer of the formimino intermediates between the active sites of the formiminotransferase-cyclodeaminase enzyme complex, with complete "channeling" of the pentaglutamate ?
-
?

Organism

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

Source Tissue

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.3.1.4 (6S)-5-formimino-5,6,7,8-tetrahydropteroylglutamate
-
Sus scrofa ?
-
?
4.3.1.4 (6S)-5-formimino-5,6,7,8-tetrahydropteroylheptaglutamate
-
Sus scrofa ?
-
?
4.3.1.4 (6S)-5-formimino-5,6,7,8-tetrahydropteroylhexaglutamate
-
Sus scrofa ?
-
?
4.3.1.4 (6S)-5-formimino-5,6,7,8-tetrahydropteroylpentaglutamate
-
Sus scrofa ?
-
?
4.3.1.4 (6S)-5-formimino-5,6,7,8-tetrahydropteroyltetraglutamate
-
Sus scrofa ?
-
?
4.3.1.4 (6S)-5-formimino-5,6,7,8-tetrahydropteroyltriglutamate
-
Sus scrofa ?
-
?
4.3.1.4 5-formiminotetrahydrofolate
-
Sus scrofa 5,10-methenyltetrahydrofolate + NH3
-
?
4.3.1.4 5-formiminotetrahydrofolate
-
Sus scrofa ?
-
?
4.3.1.4 additional information
-
Sus scrofa ?
-
?
4.3.1.4 additional information folate-dependent bifunctional enzyme formiminoglutamate: tetrahydrofolate formiminotransferase-formiminotetrahydrofolate cyclodeaminase catalyzes two sequential reactions of the histidine degradation pathway Sus scrofa ?
-
?
4.3.1.4 additional information direct transfer of the formimino intermediates between the active sites of the formiminotransferase-cyclodeaminase enzyme complex, with complete "channeling" of the pentaglutamate Sus scrofa ?
-
?

Subunits

EC Number Subunits Comment Organism
4.3.1.4 octamer formiminotransferase-cyclodeaminase enzyme complex is composed of eight subunits arranged in a planar ring Sus scrofa