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Literature summary for 1.16.3.1 extracted from

  • Haikarainen, T.; Thanassoulas, A.; Stavros, P.; Nounesis, G.; Haataja, S.; Papageorgiou, A.C.
    Structural and thermodynamic characterization of metal ion binding in Streptococcus suis Dpr (2011), J. Mol. Biol., 405, 448-460.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
D47A interactions of mutant D74A with various divalent ions compared to the wild-type enzyme, overview Streptococcus suis

Organism

Organism UniProt Comment Textmining
Streptococcus suis
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the divalent metal ions Zn2+, Mn2+, Ni2+, Co2+, and Cu2+ all bind to the ferroxidase center similarly to Fe2+, with moderate affinity, while Mg2+ does not. SsDpr is able to bind various metals as substitutes for iron, enzyme-metal complex structure, overview Streptococcus suis ?
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?

Synonyms

Synonyms Comment Organism
Dpr
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Streptococcus suis
Dps-like peroxide resistance protein
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Streptococcus suis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
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assay at Streptococcus suis

General Information

General Information Comment Organism
additional information Dps-like, i.e. DNA-binding protein from starved cells-like, proteins belong to the ferritin superfamily. They form 12-mers instead of 24-mers, in contrast to ferritins, and have a different ferroxidase center, and are able to store a smaller amount of about 500 iron atoms in a hollow cavity Streptococcus suis