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) Drosophila melanogaster

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:
Drosophila melanogaster
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: Drosophila melanogaster
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
caeruloplasmin
-
-
-
-
ceruloplasmin
-
-
-
-
ferro:O2 oxidoreductase
-
-
-
-
ferroxidase I
-
-
-
-
ferroxidase, iron II:oxygen oxidoreductase
-
-
-
-
iron(II): oxygen oxidoreductase
-
-
-
-
multicopper oxidase-1
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
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
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
MCO1 has ferroxidase activity
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 8
-
highest activity
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
basal surface of midgut
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
-
knockdown of MCO1 is correlated with increased longevity on high-iron food and decreased iron accumulation
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
FRDA_DROME
190
0
20922
Swiss-Prot
Mitochondrion (Reliability: 1)
H1UUD2_DROME
169
0
19242
TrEMBL
other Location (Reliability: 1)
A0A0B4KHF0_DROME
236
0
26195
TrEMBL
Secretory Pathway (Reliability: 1)
Q7KMQ5_DROME
180
0
20496
TrEMBL
other Location (Reliability: 1)
Q8I0T0_DROME
121
0
13604
TrEMBL
Secretory Pathway (Reliability: 1)
Q9U7A3_DROME
227
0
25276
TrEMBL
Secretory Pathway (Reliability: 1)
Q9U4U2_DROME
227
0
25270
TrEMBL
Secretory Pathway (Reliability: 1)
A1Z6F4_DROME
784
0
87243
TrEMBL
Secretory Pathway (Reliability: 4)
Q9VYH1_DROME
186
0
21411
TrEMBL
Mitochondrion (Reliability: 4)
Q9VLC3_DROME
959
0
108460
TrEMBL
other Location (Reliability: 4)
Q7JQF6_DROME
784
0
86620
TrEMBL
Secretory Pathway (Reliability: 4)
Q9VX11_DROME
645
0
72834
TrEMBL
Secretory Pathway (Reliability: 1)
Q9VA83_DROME
227
0
25242
TrEMBL
Secretory Pathway (Reliability: 1)
B7YZT1_DROME
784
0
86761
TrEMBL
Secretory Pathway (Reliability: 4)
A0A0B4KF30_DROME
784
0
87107
TrEMBL
Secretory Pathway (Reliability: 4)
B8A405_DROME
242
0
27608
TrEMBL
Secretory Pathway (Reliability: 2)
A1Z6F6_DROME
749
0
82680
TrEMBL
other Location (Reliability: 2)
Q9VBK7_DROME
677
0
77620
TrEMBL
Mitochondrion (Reliability: 2)
A0A0B4KI27_DROME
245
0
27896
TrEMBL
Secretory Pathway (Reliability: 1)
Q7KRU8_DROME
205
0
23146
TrEMBL
Secretory Pathway (Reliability: 1)
B9EQV2_DROME
229
0
26243
TrEMBL
other Location (Reliability: 3)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
R454A
-
Arg454 is mutated to Ala in order to reduce proteolytic cleavage
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
using concanavalin-A-Sepharose and Q-sepharose
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinantly expressed in Sf9 cells using the baculovirus expression system. Recombinant MCO1 is expressed without the von Willebrand factor domains and transmembrane segment, and Arg454 is mutated to alanine to reduce proteolytic cleavage
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lang, M.; Braun, C.L.; Kanost, M.R.; Gorman, M.J.
Multicopper oxidase-1 is a ferroxidase essential for iron homeostasis in Drosophila melanogaster
Proc. Natl. Acad. Sci. USA
109
13337-13342
2012
Drosophila melanogaster
Manually annotated by BRENDA team