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1.16.3.1: ferroxidase

This is an abbreviated version!
For detailed information about ferroxidase, go to the full flat file.

Word Map on EC 1.16.3.1

Reaction

4 Fe(II) + 4 H+ +

O2
= 4 Fe(III) + 2 H2O

Synonyms

AfFtn, apoferritin, bacterial ferritin, bacterial ferroxidase, bacterioferritin, bacterioferritin B, BFR, BfrB, blue copper oxidase, caeruloplasmin, ceruloplasmin, Cp115, Cp135, Cp200, CT1740, CtFtn, cyto-FOX, cytosolic FOX, DdBfr, Dpr, Dps, Dps protein, Dps-like peroxide resistance protein, Dps-Te, DpsA, DpsA-Te, DspA, EncA, encapsulin, encapsulin A, ferritin, ferro-O2-oxidoreductase, ferro:O2 oxidoreductase, ferroxidase, ferroxidase center of bacterioferritin, ferroxidase I, ferroxidase II, ferroxidase, iron II:oxygen oxidoreductase, Fet3, FET3 gene product, fet3p, FOX1, Ftn, FtnA, H ferritin, H' ferritin, H-chain ferritin, Helicobacter pylori neutrophil-activating protein, hephaestin, HP-NAP, HuHF, human ceruloplasmin form I, human H ferritin, human H-chain ferritin, iron(II): oxygen oxidoreductase, L-ferritin, M ferritin, MaDps, MCO1, MmcO, mnxDEFG, monophenol-o-monoxygenase, More, mouse ceruloplasmin, multicopper ferroxidase, multicopper oxidase, multicopper oxidase 1, multicopper oxidase CueO, multicopper oxidase-1, mushroom tyrosinase, mycobacterial multicopper oxidase, neutrophil-activating protein, non-ceruloplasmin ferroxidase, non-specific DNA-binding protein Dps/ferroxidase, rhHp, rHuHF, Rv0846c, serum ferroxidase, VcDps, VCE_000308, xanthine oxidoreductase

ECTree

     1 Oxidoreductases
         1.16 Oxidizing metal ions
             1.16.3 With oxygen as acceptor
                1.16.3.1 ferroxidase

Molecular Weight

Molecular Weight on EC 1.16.3.1 - ferroxidase

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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100000
-
2 differentially glycosylated forms, SDS-PAGE
100000 - 150000
-
glycerol gradient
100000 - 200000
-
gel filtration
113000
-
amino acid composition
114900
115000
-
human ceruloplasmin antibody reaction
120000
121000
121300
-
gel filtration
123000
-
sedimentation-velocity
124000
125000
-
amino acid composition
129000
-
determination of peptide chain length
129600
-
x * 129600, MALDI-TOF of recombinant glycoprotein, x * 143000, SDS-PAGE of recombinant protein, x * 121000, SDS-PAGE of PNGase F-treated protein
130000
131000
-
sedimentation equilibrium
132000
134000
135000
137000
-
gel filtration
140000
-
nonreducing SDS-PAGE
143000
-
x * 129600, MALDI-TOF of recombinant glycoprotein, x * 143000, SDS-PAGE of recombinant protein, x * 121000, SDS-PAGE of PNGase F-treated protein
145000
-
-
150000
155000
-
sedimentation equilibrium
158000
-
sedimentation velocity experiments
15900
-
2 * 15900 + 2 * 58900, SDS-PAGE
16000
160000
17000
-
1 * 17000 + 1 * 59000
18650
-
1 * 18650 + 1 * 50000 + 1 * 70000, limited proteolysis
19000
200000
-
human ceruloplasmin antibody reaction
20900
Thermosynechococcus vestitus
12 * 20900, about, sequence calculation, three-dimensional structure analysis of DspA-Te, the subunits forming the pores at the ferritin-like interfaces have a slightly different orientation with respect to the three-fold symmetry axes than in the other Dps structures, overview. DpsA-Te ferroxidase center is unique, owing to the presence of a His78 in place of the canonical Asp metal ligand
24000
-
1 * 24000 + 1 * 93000, cleaved by protease
25000
-
1 * 19000 + 1 * 25000 + 1 * 26000 + 1 * 67000, SDS-PAGE
26000
-
1 * 19000 + 1 * 25000 + 1 * 26000 + 1 * 67000, SDS-PAGE
35000
-
2 * 16000 + 2 * 35000, SDS-PAGE
480000
-
about, gel filtration, wild-type enzyme and mutant E57A/E136A/D140A
50000
58900
-
2 * 15900 + 2 * 58900, SDS-PAGE
59000
61800
-
protein characterization
67000
70000
-
1 * 18650 + 1 * 50000 + 1 * 70000, limited proteolysis
72400
-
calculated from amino acid sequence
72870
-
electrospray mass spectrometry
800000 - 2000000
-
ferroxidase II, gel filtration
85000
90000
-
1 * 50000 + 1 * 90000 + 1 * 50000, SDS-PAGE
93000
-
1 * 24000 + 1 * 93000, cleaved by protease