KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | network-weaving algorithm that passes threads of an allosteric network through highly correlated residues using hierarchical clustering, the residue-residue correlations are calculated, modeling, overview. The ferritin structures evolved in a way to limit the influence of functionally unrelated events in the cytoplasm on the allosteric network to maintain stability of the translocation mechanisms, allosteric mechanisms observed among homologous proteins, overview | Pseudomonas aeruginosa | |
additional information | - |
additional information | network-weaving algorithm that passes threads of an allosteric network through highly correlated residues using hierarchical clustering, the residue-residue correlations are calculated, modeling, overview. The ferritin structures evolved in a way to limit the influence of functionally unrelated events in the cytoplasm on the allosteric network to maintain stability of the translocation mechanisms, allosteric mechanisms observed among homologous proteins, overview | Lithobates catesbeianus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
2 Fe(II) + H2O2 + 2 H2O | Pseudomonas aeruginosa | - |
2 [FeO(OH)] + 4 H+ | - |
? | |
2 Fe(II) + H2O2 + 2 H2O | Lithobates catesbeianus | - |
2 [FeO(OH)] + 4 H+ | - |
? | |
2 Fe(II) + O2 + 4 H2O | Pseudomonas aeruginosa | - |
2 [FeO(OH)] + 4 H+ + H2O2 | - |
? | |
2 Fe(II) + O2 + 4 H2O | Lithobates catesbeianus | - |
2 [FeO(OH)] + 4 H+ + H2O2 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Lithobates catesbeianus | - |
- |
- |
Pseudomonas aeruginosa | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
2 Fe(II) + H2O2 + 2 H2O | - |
Pseudomonas aeruginosa | 2 [FeO(OH)] + 4 H+ | - |
? | |
2 Fe(II) + H2O2 + 2 H2O | - |
Lithobates catesbeianus | 2 [FeO(OH)] + 4 H+ | - |
? | |
2 Fe(II) + O2 + 4 H2O | - |
Pseudomonas aeruginosa | 2 [FeO(OH)] + 4 H+ + H2O2 | - |
? | |
2 Fe(II) + O2 + 4 H2O | - |
Lithobates catesbeianus | 2 [FeO(OH)] + 4 H+ + H2O2 | - |
? |
Subunits | Comment | Organism |
---|---|---|
multimer | Ftns and Bfrs proteins consist of 24 subunits that form a spherical shell, structure analysis and modeling | Pseudomonas aeruginosa |
multimer | Ftns and Bfrs proteins consist of 24 subunits that form a spherical shell, structure analysis and modeling | Lithobates catesbeianus |
Synonyms | Comment | Organism |
---|---|---|
bacterial ferritin | - |
Pseudomonas aeruginosa |
bacterioferritin | - |
Pseudomonas aeruginosa |
BfrB | - |
Pseudomonas aeruginosa |
Ftn | - |
Lithobates catesbeianus |
FtnA | - |
Pseudomonas aeruginosa |
L-ferritin | - |
Lithobates catesbeianus |
M ferritin | - |
Lithobates catesbeianus |
General Information | Comment | Organism |
---|---|---|
evolution | the ferritin (Ftn) and bacterioferritin (Bfr) proteins of the ferritin-like superfamily constitute a prime example of a remarkable combination of evolutionary conserved iron uptake and release processes that are integrated with a variety in iron translocation mechanisms. Ftns and Bfrs have a highly conserved architecture | Pseudomonas aeruginosa |
evolution | the ferritin (Ftn) and bacterioferritin (Bfr) proteins of the ferritin-like superfamily constitute a prime example of a remarkable combination of evolutionary conserved iron uptake and release processes that are integrated with a variety in iron translocation mechanisms. Ftns and Bfrs have a highly conserved architecture | Lithobates catesbeianus |
physiological function | ferritin and ferritin-like molecules (Bfr and bacterial Ftn) are supramolecular assemblies built from 24 subunits into a nearly spherical architecture with a hollow core where up to 4000 iron ions can be stored as a ferric mineral that is protected from indiscriminant cellular reducing agents. The enzymes possess an integrated ferroxidase activity, EC 1.16.3.1. . Network-weaving algorithm that passes threads of an allosteric network through highly correlated residues using hierarchical clustering, the residue-residue correlations are calculated, modeling, overview. The ferritin structures evolved in a way to limit the influence of functionally unrelated events in the cytoplasm on the allosteric network to maintain stability of the translocation mechanisms. Diversity in mechanisms of iron traffic, overview. It is thought that iron translocation across the ferritin shell requires cooperative motions of residues aligning the path. In the process of iron capture and storage, iron traverses from the ferritin exterior surface to the interior cavity via a ferroxidase center, where soluble Fe2+ is oxidized to Fe3+. A ferroxidase center is located in the middle of each subunit in the heavy (H)-type and M-type subunits of eukaryotic Ftns. Release of iron from the ferritin cavity requires reduction of ferric iron in the interior ferritin cavity and egress of ferrous ions via pores in the protein shell. The networks in BfrB and FtnA connect the ferroxidase center with the 4fold pores and B-pores, leaving the 3fold pores unengaged | Lithobates catesbeianus |
physiological function | ferritin and ferritin-like molecules (Bfr and bacterial Ftn) are supramolecular assemblies built from 24 subunits into a nearly spherical architecture with a hollow core where up to 4000 iron ions can be stored as a ferric mineral that is protected from indiscriminant cellular reducing agents. The enzymes possess an integrated ferroxidase activity, EC 1.16.3.1. Network-weaving algorithm that passes threads of an allosteric network through highly correlated residues using hierarchical clustering, the residue-residue correlations are calculated, modeling, overview. Each type of ferritin-like molecule has an extended network of highly correlated residues, connecting distant pores and the ferroxidase center. The ferritin structures evolved in a way to limit the influence of functionally unrelated events in the cytoplasm on the allosteric network to maintain stability of the translocation mechanisms. Diversity in mechanisms of iron traffic, overview. It is thought that iron translocation across the ferritin shell requires cooperative motions of residues aligning the path. In the process of iron capture and storage, iron traverses from the ferritin exterior surface to the interior cavity via a ferroxidase center, where soluble Fe2+ is oxidized to Fe3+. A ferroxidase center is located in the middle of each subunit in Bfrs. Release of iron from the ferritin cavity requires reduction of ferric iron in the interior ferritin cavity and egress of ferrous ions via pores in the protein shell. The networks in BfrB and FtnA connect the ferroxidase center with the 4fold pores and B-pores, leaving the 3fold pores unengaged | Pseudomonas aeruginosa |
physiological function | ferritin and ferritin-like molecules (Bfr and bacterial Ftn) are supramolecular assemblies built from 24 subunits into a nearly spherical architecture with a hollow core where up to 4000 iron ions can be stored as a ferric mineral that is protected from indiscriminant cellular reducing agents. The enzymes possess an integrated ferroxidase activity, EC 1.16.3.1. Network-weaving algorithm that passes threads of an allosteric network through highly correlated residues using hierarchical clustering, the residue-residue correlations are calculated, modeling, overview. Each type of ferritin-like molecule has an extended network of highly correlated residues, connecting distant pores and the ferroxidase center. The ferritin structures evolved in a way to limit the influence of functionally unrelated events in the cytoplasm on the allosteric network to maintain stability of the translocation mechanisms. Diversity in mechanisms of iron traffic, overview. It is thought that iron translocation across the ferritin shell requires cooperative motions of residues aligning the path. In the process of iron capture and storage, iron traverses from the ferritin exterior surface to the interior cavity via a ferroxidase center, where soluble Fe2+ is oxidized to Fe3+. A ferroxidase center is located in the middle of each subunit in bacterial Ftn. Release of iron from the ferritin cavity requires reduction of ferric iron in the interior ferritin cavity and egress of ferrous ions via pores in the protein shell. The networks in BfrB and FtnA connect the ferroxidase center with the 4fold pores and B-pores, leaving the 3fold pores unengaged | Pseudomonas aeruginosa |