Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.16.3.1 extracted from

  • Haikarainen, T.; Tsou, C.C.; Wu, J.J.; Papageorgiou, A.C.
    Structural characterization and biological implications of di-zinc binding in the ferroxidase center of Streptococcus pyogenes Dpr (2010), Biochem. Biophys. Res. Commun., 398, 361-365.
    View publication on PubMed
Search for more literature for 1.16.3.1

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression in Escherichia coli Streptococcus pyogenes

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant Dpr in complex with Zn2+, hanging drop vapour diffusion method, protein in 1 M succinic acid, 5% 2-propanol, and 1% w/v PEG 2000 MME, X-ray diffraction structure determination and analysis at 2.1 A resolution Streptococcus pyogenes

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Streptococcus pyogenes Dps proteins oxidize Fe2+ to Fe3+ using 12 ferroxidase centers, each of them located at a dimer interface ?
-
 ?

Organism

Organism UniProt Comment Textmining
Streptococcus pyogenes
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme from Escherichia coli Streptococcus pyogenes

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information Dps proteins oxidize Fe2+ to Fe3+ using 12 ferroxidase centers, each of them located at a dimer interface Streptococcus pyogenes ?
-
 ?
additional information Dpr is also able to bind zinc as an oxidation stable replacement for iron, metal complex binding structure, formation of a di-zinc center, a third zinc ion is found on the surface of the protein, overview Streptococcus pyogenes ?
-
 ?

Subunits

Subunits Comment Organism
dimer Dps proteins structure comparisons, overview Streptococcus pyogenes

Synonyms

Synonyms Comment Organism
Dpr
-
 Streptococcus pyogenes
Dps i.e. DNA-binding proteins from starved cells Streptococcus pyogenes
Dps-like peroxide resistance protein
-
 Streptococcus pyogenes

General Information

General Information Comment Organism
physiological function Dps proteins contain a ferroxidase site that binds and oxidizes iron, thereby consuming H2O2 and preventing hydroxyl radical formation by Fenton reaction. Dps proteins oxidize Fe2+ to Fe3+ using 12 ferroxidase centers, each of them located at a dimer interface Streptococcus pyogenes