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Literature summary extracted from

  • Murley, L.L.; MacKenzie, R.E.
    The two monofunctional domains of octameric formiminotransferase-cyclodeaminase exist as dimers (1995), Biochemistry, 34, 10358-10364.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.1.2.5 expression of full-length formiminotransferase cyclodeaminase and of isolated N-terminal transferase and C-terminal deaminase domains in Escherichia coli BL21/DE3 as His-tagged proteins Sus scrofa

Protein Variants

EC Number Protein Variants Comment Organism
2.1.2.5 additional information deletion mutants of formiminotransferase cyclodeaminase with transferase activity Sus scrofa

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.1.2.5 0.0017
-
 (6S)-tetrahydropteroylpentaglutamate recombinant His-tagged bifunctional formiminotransferase cyclodeaminase Sus scrofa
2.1.2.5 0.075
-
 (6S)-tetrahydropteroylpentaglutamate recombinant His-tagged formiminotransferase domain Sus scrofa
2.1.2.5 0.111
-
 (6R,S)-tetrahydrofolate recombinant His-tagged formiminotransferase domain Sus scrofa
2.1.2.5 0.141
-
 (6R,S)-tetrahydrofolate wild-type bifunctional formiminotransferase cyclodeaminase Sus scrofa
2.1.2.5 0.148
-
 (6R,S)-tetrahydrofolate recombinant His-tagged bifunctional formiminotransferase cyclodeaminase Sus scrofa
2.1.2.5 5.8
-
 N-formimino-L-glutamate wild-type bifunctional formiminotransferase cyclodeaminase Sus scrofa
2.1.2.5 6.7
-
 N-formimino-L-glutamate recombinant His-tagged bifunctional formiminotransferase cyclodeaminase Sus scrofa
2.1.2.5 8.3
-
 N-formimino-L-glutamate recombinant His-tagged formiminotransferase domain Sus scrofa

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.1.2.5 37000
-
 2 * 37000, recombinant His-tagged N-terminal formiminotransferase domain of bifunctional formiminotransferase cyclodeaminase, calculated from the amino acid sequence Sus scrofa
2.1.2.5 83000
-
 recombinant His-tagged N-terminal formiminotransferase domain of bifunctional formiminotransferase cyclodeaminase, gel filtration Sus scrofa
2.1.2.5 380000
-
 recombinant His-tagged bifunctional formiminotransferase cyclodeaminase, gel filtration Sus scrofa
2.1.2.5 438000
-
 wild-type bifunctional formiminotransferase cyclodeaminase, gel filtration Sus scrofa

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.1.2.5 N-formiminoglutamate + tetrahydrofolate Sus scrofa enzyme serves as additional entry point for the folate pool in liver 5-formiminotetrahydrofolate + L-glutamate
-
 ?
2.1.2.5 N-formiminoglutamate + tetrahydrofolate Sus scrofa histidine degradation 5-formiminotetrahydrofolate + L-glutamate
-
 ?

Organism

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

Purification (Commentary)

EC Number Purification (Comment) Organism
2.1.2.5 purification of wild type bifunctional formiminotransferase cyclodeaminase, 150fold purification of His-tagged recombinant enzyme, 60fold purification of His-tagged transferase domain, expressed in Escherichia coli BL21/DE3 Sus scrofa

Source Tissue

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.2.5 (6R,S)-tetrahydrofolate + N-formimidoyl-L-glutamate
-
 Sus scrofa 5-formimidoyltetrahydrofolate + L-glutamate
-
 r
2.1.2.5 (6S)-tetrahydropteroylpentaglutamate + N-formimidoyl-L-glutamate
-
 Sus scrofa 5-formiminotetrahydropteroylpentaglutamate + L-glutamate
-
 r
2.1.2.5 additional information FTCD: bifunctional enzyme formiminotransferase cyclodeaminase efficiently channels polyglutamated folate between catalytic sites, only the octamer is able to directly transfer pentaglutamated intermediate between active sites, subunit structure Sus scrofa ?
-
 ?
2.1.2.5 N-formiminoglutamate + tetrahydrofolate enzyme serves as additional entry point for the folate pool in liver Sus scrofa 5-formiminotetrahydrofolate + L-glutamate
-
 ?
2.1.2.5 N-formiminoglutamate + tetrahydrofolate histidine degradation Sus scrofa 5-formiminotetrahydrofolate + L-glutamate
-
 ?
2.1.2.5 tetrahydrofolate + N-formimino-L-glutamate transfer of a single carbon from formiminoglutamate to tetrahydrofolate, product is 5-formiminotetrahydrofolate Sus scrofa 5-formiminotetrahydrofolate + L-glutamate
-
 ?
2.1.2.5 tetrahydropteroylpentaglutamate + N-formimino-L-glutamate bifunctional formiminotetrahydrofolate cyclodeaminase: preference for polyglutamylated substrates, polyglutamylation improves binding of both the folate substrates and formiminoglutamate Sus scrofa 5-formiminotetrahydropteroylpentaglutamate + L-glutamate
-
 ?

Subunits

EC Number Subunits Comment Organism
2.1.2.5 dimer 2 * 37000, recombinant His-tagged N-terminal formiminotransferase domain of bifunctional formiminotransferase cyclodeaminase, calculated from the amino acid sequence Sus scrofa
2.1.2.5 octamer 8 * 59000-60000, bifunctional formiminotransferase cyclodeaminase, calculated from the amino acid sequence, circular tetramer of dimers, each subunit consists of an N-terminal transferase active domain and a C-terminal deaminase active domain separated by a linker sequence of 8-12 residues, both domains self-dimerize: existence of two types of subunit interfaces, transferase and deaminase activities are dependent on the formation of specific subunit interfaces Sus scrofa

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.1.2.5 additional information
-
 additional information 3480-4620 per min: bifunctional formiminotransferase cyclodeaminase, 1920 per min: recombinant His-tagged formiminotransferase domain Sus scrofa

Cofactor

EC Number Cofactor Comment Organism Structure
2.1.2.5 tetrahydrofolate folate-dependent enzyme Sus scrofa