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

BRENDA support

Literature summary for 1.16.3.1 extracted from

  • Zeth, K.; Hoiczyk, E.; Okuda, M.
    Ferroxidase-mediated iron oxide biomineralization novel pathways to multifunctional nanoparticles (2016), Trends Biochem. Sci., 41, 190-203 .
    View publication on PubMed

Application

Application Comment Organism
biotechnology compartmentalized iron oxide biomineralization by the enzyme yields uniform nanoparticles strictly determined by the sizes of the compartments, allowing customization for highly diverse nanotechnological applications Microbacterium arborescens
biotechnology compartmentalized iron oxide biomineralization by the enzyme yields uniform nanoparticles strictly determined by the sizes of the compartments, allowing customization for highly diverse nanotechnological applications Myxococcus xanthus
biotechnology compartmentalized iron oxide biomineralization by the enzyme yields uniform nanoparticles strictly determined by the sizes of the compartments, allowing customization for highly diverse nanotechnological applications Thermotoga maritima
biotechnology compartmentalized iron oxide biomineralization by the enzyme yields uniform nanoparticles strictly determined by the sizes of the compartments, allowing customization for highly diverse nanotechnological applications Halobacterium salinarum
biotechnology compartmentalized iron oxide biomineralization by the enzyme yields uniform nanoparticles strictly determined by the sizes of the compartments, allowing customization for highly diverse nanotechnological applications Vibrio cholerae
biotechnology compartmentalized iron oxide biomineralization by the enzyme yields uniform nanoparticles strictly determined by the sizes of the compartments, allowing customization for highly diverse nanotechnological applications Streptomyces coelicolor

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structure analysis, PDB ID 1TJO Halobacterium salinarum
crystal structure analysis, PDB ID 3DKT Thermotoga maritima
crystal structure analysis, PDB ID 4PT2 Myxococcus xanthus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4 Fe(II) + 4 H+ + O2 Microbacterium arborescens
-
4 Fe(III) + 2 H2O
-
?
4 Fe(II) + 4 H+ + O2 Myxococcus xanthus
-
4 Fe(III) + 2 H2O
-
?
4 Fe(II) + 4 H+ + O2 Thermotoga maritima
-
4 Fe(III) + 2 H2O
-
?
4 Fe(II) + 4 H+ + O2 Halobacterium salinarum
-
4 Fe(III) + 2 H2O
-
?
4 Fe(II) + 4 H+ + O2 Vibrio cholerae
-
4 Fe(III) + 2 H2O
-
?
4 Fe(II) + 4 H+ + O2 Streptomyces coelicolor
-
4 Fe(III) + 2 H2O
-
?
4 Fe(II) + 4 H+ + O2 Vibrio cholerae B33
-
4 Fe(III) + 2 H2O
-
?
4 Fe(II) + 4 H+ + O2 Myxococcus xanthus DK 1622
-
4 Fe(III) + 2 H2O
-
?
4 Fe(II) + 4 H+ + O2 Streptomyces coelicolor ATCC BAA-471 / A3(2) / M145
-
4 Fe(III) + 2 H2O
-
?
4 Fe(II) + 4 H+ + O2 Halobacterium salinarum ATCC 29341
-
4 Fe(III) + 2 H2O
-
?

Organism

Organism UniProt Comment Textmining
Halobacterium salinarum B0R7W1
-
-
Halobacterium salinarum ATCC 29341 B0R7W1
-
-
Microbacterium arborescens
-
-
-
Myxococcus xanthus Q1D6H4
-
-
Myxococcus xanthus DK 1622 Q1D6H4
-
-
Streptomyces coelicolor Q9R408
-
-
Streptomyces coelicolor ATCC BAA-471 / A3(2) / M145 Q9R408
-
-
Thermotoga maritima Q9WZP2
-
-
Vibrio cholerae A0A0H3Q5A5
-
-
Vibrio cholerae B33 A0A0H3Q5A5
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4 Fe(II) + 4 H+ + O2
-
Microbacterium arborescens 4 Fe(III) + 2 H2O
-
?
4 Fe(II) + 4 H+ + O2
-
Myxococcus xanthus 4 Fe(III) + 2 H2O
-
?
4 Fe(II) + 4 H+ + O2
-
Thermotoga maritima 4 Fe(III) + 2 H2O
-
?
4 Fe(II) + 4 H+ + O2
-
Halobacterium salinarum 4 Fe(III) + 2 H2O
-
?
4 Fe(II) + 4 H+ + O2
-
Vibrio cholerae 4 Fe(III) + 2 H2O
-
?
4 Fe(II) + 4 H+ + O2
-
Streptomyces coelicolor 4 Fe(III) + 2 H2O
-
?
4 Fe(II) + 4 H+ + O2
-
Vibrio cholerae B33 4 Fe(III) + 2 H2O
-
?
4 Fe(II) + 4 H+ + O2
-
Myxococcus xanthus DK 1622 4 Fe(III) + 2 H2O
-
?
4 Fe(II) + 4 H+ + O2
-
Streptomyces coelicolor ATCC BAA-471 / A3(2) / M145 4 Fe(III) + 2 H2O
-
?
4 Fe(II) + 4 H+ + O2
-
Halobacterium salinarum ATCC 29341 4 Fe(III) + 2 H2O
-
?

Subunits

Subunits Comment Organism
dimer dodecamer or dimer, structure analysis, overview Halobacterium salinarum
dodecamer
-
Streptomyces coelicolor
dodecamer structure analysis, overview Microbacterium arborescens
dodecamer structure analysis, overview Vibrio cholerae
dodecamer dodecamer or dimer, structure analysis, overview Halobacterium salinarum
More structure analysis, overview Myxococcus xanthus
More structure analysis, overview Thermotoga maritima

Synonyms

Synonyms Comment Organism
bacterial ferroxidase
-
Microbacterium arborescens
bacterial ferroxidase
-
Myxococcus xanthus
bacterial ferroxidase
-
Thermotoga maritima
bacterial ferroxidase
-
Halobacterium salinarum
bacterial ferroxidase
-
Vibrio cholerae
bacterial ferroxidase
-
Streptomyces coelicolor
DspA
-
Halobacterium salinarum
DspA
-
Streptomyces coelicolor
EncA
-
Myxococcus xanthus
encapsulin
-
Thermotoga maritima
encapsulin A
-
Myxococcus xanthus
ferritin
-
Halobacterium salinarum
ferritin
-
Streptomyces coelicolor
MaDps
-
Microbacterium arborescens
non-specific DNA-binding protein Dps/ferroxidase UniProt Vibrio cholerae
VcDps
-
Vibrio cholerae
VCE_000308 gene name, UniProt Vibrio cholerae

General Information

General Information Comment Organism
additional information Dps protein structure and mechanism for ferroxidase-mediated biomineralization, overview Microbacterium arborescens
additional information Dps protein structure and mechanism for ferroxidase-mediated biomineralization, overview. Vibrio cholerae Dps (VcDps) and DpsA representing type I and II channels Vibrio cholerae
additional information encapsulin A is comprising 180 virus-like structural proteins with an outer diameter of 32 nm. Mechanism for ferroxidase-mediated biomineralization, overview Myxococcus xanthus
additional information encapsulin is comprising 60 virus-like structural proteins with an outer diameter of 24 nm. Mechanism for ferroxidase-mediated biomineralization, overview Thermotoga maritima
additional information in the dodecameric Dps, translocation position T3 is located at the channel exit where conserved Asp residues narrow the pore diameter significantly, forming a scaffold for tethering ions at the inner wall of the protein. After crossing the constriction zone, three ferroxidase centers are located about 20 A apart and iron can move along negatively charged residues at the inner wall towards the ferroxidase center with high-affinity binding. Mechanism for ferroxidase-mediated biomineralization, overview Streptomyces coelicolor
additional information the dodecameric Dps protein with an outer particle radius of 8 nm and a storage capacity of about 500 iron atoms. Ferritin can be assembled using six tetramers per cubic face, while Dps complexes are formed through the assembly of six protein dimers on each plane of the cube. Mechanism for ferroxidase-mediated biomineralization, overview Halobacterium salinarum
physiological function ferroxidase-mediated iron oxide biomineralization. The formation of iron-oxo particles in all these compartments requires a series of steps including recruitment of iron, translocation, oxidation, nucleation, and storage, that are mediated by ferroxidase centers. Compartmentalized iron oxide biomineralization yields uniform nanoparticles strictly determined by the sizes of the compartments. Dps, ferritin, and encapsulin all form protein-coated minerals of variable small sizes with similar iron oxide composition Microbacterium arborescens
physiological function ferroxidase-mediated iron oxide biomineralization. The formation of iron-oxo particles in all these compartments requires a series of steps including recruitment of iron, translocation, oxidation, nucleation, and storage, that are mediated by ferroxidase centers. Compartmentalized iron oxide biomineralization yields uniform nanoparticles strictly determined by the sizes of the compartments. Dps, ferritin, and encapsulin all form protein-coated minerals of variable small sizes with similar iron oxide composition Myxococcus xanthus
physiological function ferroxidase-mediated iron oxide biomineralization. The formation of iron-oxo particles in all these compartments requires a series of steps including recruitment of iron, translocation, oxidation, nucleation, and storage, that are mediated by ferroxidase centers. Compartmentalized iron oxide biomineralization yields uniform nanoparticles strictly determined by the sizes of the compartments. Dps, ferritin, and encapsulin all form protein-coated minerals of variable small sizes with similar iron oxide composition Thermotoga maritima
physiological function ferroxidase-mediated iron oxide biomineralization. The formation of iron-oxo particles in all these compartments requires a series of steps including recruitment of iron, translocation, oxidation, nucleation, and storage, that are mediated by ferroxidase centers. Compartmentalized iron oxide biomineralization yields uniform nanoparticles strictly determined by the sizes of the compartments. Dps, ferritin, and encapsulin all form protein-coated minerals of variable small sizes with similar iron oxide composition Halobacterium salinarum
physiological function ferroxidase-mediated iron oxide biomineralization. The formation of iron-oxo particles in all these compartments requires a series of steps including recruitment of iron, translocation, oxidation, nucleation, and storage, that are mediated by ferroxidase centers. Compartmentalized iron oxide biomineralization yields uniform nanoparticles strictly determined by the sizes of the compartments. Dps, ferritin, and encapsulin all form protein-coated minerals of variable small sizes with similar iron oxide composition Vibrio cholerae
physiological function ferroxidase-mediated iron oxide biomineralization. The formation of iron-oxo particles in all these compartments requires a series of steps including recruitment of iron, translocation, oxidation, nucleation, and storage, that are mediated by ferroxidase centers. Compartmentalized iron oxide biomineralization yields uniform nanoparticles strictly determined by the sizes of the compartments. Dps, ferritin, and encapsulin all form protein-coated minerals of variable small sizes with similar iron oxide composition Streptomyces coelicolor