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Literature summary for 2.1.2.5 extracted from
- Molecular cloning, characterization, and dynamics of rat formiminotransferase cyclodeaminase, a Golgi-associated 58-kDa protein (1998), J. Biol. Chem., 273, 33825-33834.
Application
| Application | Comment | Organism |
|---|---|---|
| molecular biology | bifunctional formiminotransferase cyclodeaminase provides a novel marker to study ER-Golgi dynamics | Rattus norvegicus |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| cDNA encoding formiminotransferase cyclodeaminase is cloned, characterized and partially sequenced | Rattus norvegicus |
General Stability
| General Stability | Organism |
|---|---|
| dimeric, tetrameric and octameric complexes are resistant to proteolysis | Rattus norvegicus |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| proteinase K | degradation of bifunctional formiminotransferase cyclodeaminase | Rattus norvegicus | |
| Urea | degradation of bifunctional formiminotransferase cyclodeaminase | Rattus norvegicus |  |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| 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 | - |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 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 |
| 58000 | - |
4 * 58000, bifunctional formiminotransferase cyclodeaminase exists as dimeric, tetrameric and octameric complexes, SDS-PAGE | Rattus norvegicus |
| 58000 | - |
8 * 58000, bifunctional formiminotransferase cyclodeaminase exists as dimeric, tetrameric and octameric complexes, SDS-PAGE | Rattus norvegicus |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 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 | - |
? | |
| N-formiminoglutamate + tetrahydrofolate | Rattus norvegicus | metabolic enzyme involved in the conversion of histidine to glutamic acid | 5-formiminotetrahydrofolate + L-glutamate | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Rattus norvegicus | - |
Sprague-Dawley rats | - |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| kidney | - |
Rattus norvegicus | - |
| liver | - |
Rattus norvegicus | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | 58K: formiminotransferase cyclodeaminase, bifunctional enzyme catalyzing two consecutive steps in the modification of tetrahydrofolate to 5,10-methenyl tetrahydrofolate | Rattus norvegicus | ? | - |
? | |
| 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 | - |
? | |
| N-formiminoglutamate + tetrahydrofolate | metabolic enzyme involved in the conversion of histidine to glutamic acid | Rattus norvegicus | 5-formiminotetrahydrofolate + L-glutamate | - |
? | |
| tetrahydrofolate + N-formimino-L-glutamate | - |
Rattus norvegicus | 5-formiminotetrahydrofolate + L-glutamate | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| 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 |
| octamer | 8 * 58000, bifunctional formiminotransferase cyclodeaminase exists as dimeric, tetrameric and octameric complexes, SDS-PAGE | Rattus norvegicus |
| tetramer | 4 * 58000, bifunctional formiminotransferase cyclodeaminase exists as dimeric, tetrameric and octameric complexes, SDS-PAGE | Rattus norvegicus |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| tetrahydrofolate | - |
Rattus norvegicus | |
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