EC Number | Application | Comment | Organism |
---|---|---|---|
2.1.2.5 | molecular biology | bifunctional formiminotransferase cyclodeaminase provides a novel marker to study ER-Golgi dynamics | Rattus norvegicus |
4.3.1.4 | analysis | formiminotransferase cyclodeaminase enzyme complex represents a marker with which to explore ER-Golgi dynamics | Rattus norvegicus |
EC Number | Cloned (Comment) | Organism |
---|---|---|
2.1.2.5 | cDNA encoding formiminotransferase cyclodeaminase is cloned, characterized and partially sequenced | Rattus norvegicus |
4.3.1.4 | formiminotransferase-cyclodeaminase enzyme complex | Rattus norvegicus |
EC Number | General Stability | Organism |
---|---|---|
2.1.2.5 | dimeric, tetrameric and octameric complexes are resistant to proteolysis | Rattus norvegicus |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
2.1.2.5 | proteinase K | degradation of bifunctional formiminotransferase cyclodeaminase | Rattus norvegicus | |
2.1.2.5 | Urea | degradation of bifunctional formiminotransferase cyclodeaminase | Rattus norvegicus |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
2.1.2.5 | Golgi membrane | formiminotransferase cyclodeaminase, 58K, is a peripherically associated Golgi protein, binding is tight but not dependent on presence of intact microtubules, association is likely to be mediated by a protein, dynamic component of the Golgi, a proportion of FTCD molecules cycles between the Golgi and earlier compartments of the secretory pathway | Rattus norvegicus | 139 | - |
4.3.1.4 | Golgi apparatus | Golgi apparatus, formiminotransferase-cyclodeaminase enzyme complex | Rattus norvegicus | 5794 | - |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
2.1.2.5 | 58000 | - |
2 * 58000, bifunctional formiminotransferase cyclodeaminase exists as dimeric, tetrameric and octameric complexes, SDS-PAGE, a single 35 kDa protein is cross-linked to each dimer, it may play a role in the association of the protein to the Golgi membrane, functional formiminotransferase activity unit of FTCD is a dimer with binding sites for glutamate and folate | Rattus norvegicus |
2.1.2.5 | 58000 | - |
4 * 58000, bifunctional formiminotransferase cyclodeaminase exists as dimeric, tetrameric and octameric complexes, SDS-PAGE | Rattus norvegicus |
2.1.2.5 | 58000 | - |
8 * 58000, bifunctional formiminotransferase cyclodeaminase exists as dimeric, tetrameric and octameric complexes, SDS-PAGE | Rattus norvegicus |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.1.2.5 | N-formiminoglutamate + tetrahydrofolate | Rattus norvegicus | bifunctional formiminotransferase cyclodeaminase, 58K, is associated with the cytoplasmatic surface of the Golgi apparatus in vivo | 5-formiminotetrahydrofolate + L-glutamate | - |
? | |
2.1.2.5 | N-formiminoglutamate + tetrahydrofolate | Rattus norvegicus | metabolic enzyme involved in the conversion of histidine to glutamic acid | 5-formiminotetrahydrofolate + L-glutamate | - |
? | |
4.3.1.4 | 5-formiminotetrahydrofolate | Rattus norvegicus | - |
? | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.1.2.5 | Rattus norvegicus | - |
Sprague-Dawley rats | - |
4.3.1.4 | Rattus norvegicus | - |
- |
- |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
2.1.2.5 | kidney | - |
Rattus norvegicus | - |
2.1.2.5 | liver | - |
Rattus norvegicus | - |
4.3.1.4 | liver | - |
Rattus norvegicus | - |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.1.2.5 | additional information | 58K: formiminotransferase cyclodeaminase, bifunctional enzyme catalyzing two consecutive steps in the modification of tetrahydrofolate to 5,10-methenyl tetrahydrofolate | Rattus norvegicus | ? | - |
? | |
2.1.2.5 | N-formiminoglutamate + tetrahydrofolate | bifunctional formiminotransferase cyclodeaminase, 58K, is associated with the cytoplasmatic surface of the Golgi apparatus in vivo | Rattus norvegicus | 5-formiminotetrahydrofolate + L-glutamate | - |
? | |
2.1.2.5 | N-formiminoglutamate + tetrahydrofolate | metabolic enzyme involved in the conversion of histidine to glutamic acid | Rattus norvegicus | 5-formiminotetrahydrofolate + L-glutamate | - |
? | |
2.1.2.5 | tetrahydrofolate + N-formimino-L-glutamate | - |
Rattus norvegicus | 5-formiminotetrahydrofolate + L-glutamate | - |
? | |
4.3.1.4 | 5-formiminotetrahydrofolate | - |
Rattus norvegicus | 5,10-methenyltetrahydrofolate + NH3 | - |
? | |
4.3.1.4 | 5-formiminotetrahydrofolate | - |
Rattus norvegicus | ? | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
2.1.2.5 | dimer | 2 * 58000, bifunctional formiminotransferase cyclodeaminase exists as dimeric, tetrameric and octameric complexes, SDS-PAGE, a single 35 kDa protein is cross-linked to each dimer, it may play a role in the association of the protein to the Golgi membrane, functional formiminotransferase activity unit of FTCD is a dimer with binding sites for glutamate and folate | Rattus norvegicus |
2.1.2.5 | octamer | 8 * 58000, bifunctional formiminotransferase cyclodeaminase exists as dimeric, tetrameric and octameric complexes, SDS-PAGE | Rattus norvegicus |
2.1.2.5 | tetramer | 4 * 58000, bifunctional formiminotransferase cyclodeaminase exists as dimeric, tetrameric and octameric complexes, SDS-PAGE | Rattus norvegicus |
4.3.1.4 | octamer | 8* 58000, calculation from sequence of cDNA | Rattus norvegicus |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
2.1.2.5 | tetrahydrofolate | - |
Rattus norvegicus |