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Literature summary for 1.16.3.2 extracted from

  • Ruvinsky, A.; Vakser, I.; Rivera, M.
    Local packing modulates diversity of iron pathways and cooperative behavior in eukaryotic and prokaryotic ferritins (2014), J. Chem. Phys., 140, 115104 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.16.3.2

KM Value [mM]

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/ Products (Substrates)

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

Organism UniProt Comment Textmining
Lithobates catesbeianus
-
-
-
Pseudomonas aeruginosa
-
-
-

Substrates and Products (Substrate)

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

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

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

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