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

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 1.16.3.1 - ferroxidase and Organism(s) Escherichia coli and UniProt Accession P0ABD3

for references in articles please use BRENDA:EC1.16.3.1
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
     1 Oxidoreductases
         1.16 Oxidizing metal ions
             1.16.3 With oxygen as acceptor
                1.16.3.1 ferroxidase
IUBMB Comments
The enzyme in blood plasma (ceruloplasmin) belongs to the family of multicopper oxidases. In humans it accounts for 95% of plasma copper. It oxidizes Fe(II) to Fe(III), which allows the subsequent incorporation of the latter into proteins such as apotransferrin and lactoferrin. An enzyme from iron oxidizing bacterium strain TI-1 contains heme a.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Escherichia coli
UNIPROT: P0ABD3
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
Synonyms
ferritin, ceruloplasmin, ferroxidase, apoferritin, xanthine oxidoreductase, caeruloplasmin, l-ferritin, hephaestin, bacterioferritin, hp-nap, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ferroxidase center of bacterioferritin
-
caeruloplasmin
-
-
-
-
ceruloplasmin
-
-
-
-
ferro:O2 oxidoreductase
-
-
-
-
ferroxidase I
-
-
-
-
ferroxidase, iron II:oxygen oxidoreductase
-
-
-
-
iron(II): oxygen oxidoreductase
-
-
-
-
multicopper oxidase CueO
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
Fe(II):oxygen oxidoreductase
The enzyme in blood plasma (ceruloplasmin) belongs to the family of multicopper oxidases. In humans it accounts for 95% of plasma copper. It oxidizes Fe(II) to Fe(III), which allows the subsequent incorporation of the latter into proteins such as apotransferrin and lactoferrin. An enzyme from iron oxidizing bacterium strain TI-1 contains heme a.
CAS REGISTRY NUMBER
COMMENTARY hide
9031-37-2
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4 Fe(II) + 4 H+ + O2
4 Fe(III) + 2 H2O
show the reaction diagram
Cu(II) stimulated Fe(II) oxidase activity. The enzyme also oxidizes Cu+ and is required for copper homeostasis in Escherichia coli
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cu+
Cu(I) coordinates to a flexible, methionine-rich sequence
Cu2+
stimulates Fe(II) oxidase activity
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Zn2+
50 Zn2+ ions per bacterioferritin blocked binding of Fe2+
Ag+
strongly inhibits CueO oxidase activities in vitro
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.12 - 0.135
Fe(II)
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.7 - 3.9
Fe(II)
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain JM109 and strain BL21(DE3)pLysS
UniProt
Manually annotated by BRENDA team
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
24-mer
BFR consists of 24 identical subunits arranged as 12 subunit dimers, each dimer contains a ferroxidase center, X-ray diffraction
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop method, crystal structure of CueO at 1.1 A with the 45-residue methionine-rich segment fully resolved, revealing an N-terminal helical segment with methionine residues juxtaposed for Cu(I) ligation and a C-terminal highly mobile segment rich in methionine and histidine residues. Structures of CueO with a C500S mutation, and CueO with six methionines changed to serine
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
W133F
protein is lesser sensitive to Fe2+ than wild-type protein
W35F
fluorescence spectrum is blunted compared to wild-type protein
W35F/W133F
oxidation of Fe2+ to Fe3+ is slightly reduced
C500S
mutation leads to loss of the T1 copper
M358S/M361S/M362S/M364S/M366S
mutation leads to an about 4fold reduction in kcat for Cu(I) oxidation
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli to create mutants by site-directed mutagenesis
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
CueO is only expressed when copper ions are present
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lawson, T.L.; Crow, A.; Lewin, A.; Yasmin, S.; Moore, G.R.; Le Brun, N.E.
Monitoring the iron status of the ferroxidase center of Escherichia coli bacterioferritin using fluorescence spectroscopy
Biochemistry
48
9031-9039
2009
Escherichia coli (P0ABD3), Escherichia coli
Manually annotated by BRENDA team
Singh, S.K.; Roberts, S.A.; McDevitt, S.F.; Weichsel, A.; Wildner, G.F.; Grass, G.B.; Rensing, C.; Montfort, W.R.
Crystal structures of multicopper oxidase CueO bound to copper(I) and silver(I) functional role of a methionine-rich sequence
J. Biol. Chem.
286
37849-3757
2011
Escherichia coli (P36649), Escherichia coli, Escherichia coli K12 (P36649)
Manually annotated by BRENDA team