KEGG   ENZYME: 1.16.3.1Help
Entry
EC 1.16.3.1                 Enzyme                                 

Name
ferroxidase;
ceruloplasmin;
caeruloplasmin;
ferroxidase I;
iron oxidase;
iron(II):oxygen oxidoreductase;
ferro:O2 oxidoreductase;
iron II:oxygen oxidoreductase;
hephaestin;
HEPH
Class
Oxidoreductases;
Oxidizing metal ions;
With oxygen as acceptor
BRITE hierarchy
Sysname
Fe(II):oxygen oxidoreductase
Reaction(IUBMB)
4 Fe(II) + 4 H+ + O2 = 4 Fe(III) + 2 H2O [RN:R00078]
Reaction(KEGG)
Substrate
Fe(II) [CPD:C14818];
H+ [CPD:C00080];
O2 [CPD:C00007]
Product
Fe(III) [CPD:C14819];
H2O [CPD:C00001]
Comment
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.
History
EC 1.16.3.1 created 1972, modified 2011
Pathway
Porphyrin and chlorophyll metabolism
Orthology
K13624  
ceruloplasmin
K14735  
hephaestin
Genes
HSA: 
1356(CP) 9843(HEPH)
PTR: 
465679(HEPH)
PPS: 
GGO: 
PON: 
MCC: 
709879(HEPH) 712210(CP) 714135(CP)
MCF: 
MMU: 
12870(Cp) 15203(Heph)
RNO: 
117240(Heph) 24268(Cp)
CGE: 
HGL: 
TUP: 
CFA: 
442963(CP) 491926(HEPH) 611632
AML: 
FCA: 
PTG: 
BTA: 
510736(HEPH) 514194(CP) 526230(CP)
BOM: 
PHD: 
CHX: 
OAS: 
SSC: 
CFR: 
BACU: 
LVE: 
ECB: 
MYB: 
MYD: 
PALE: 
MDO: 
SHR: 
OAA: 
GGA: 
422168(HEPH) 771940(CP)
MGP: 
TGU: 
FAB: 
PHI: 
APLA: 
FPG: 
FCH: 
CLV: 
ASN: 
AMJ: 
PSS: 
CMY: 
ACS: 
PBI: 
XTR: 
DRE: 
84702(cp)
TRU: 
MZE: 
OLA: 
XMA: 
LCM: 
CMK: 
CRE: 
VCN: 
CVR: 
NGR: 
 » show all
Taxonomy
Reference
1  [PMID:5925868]
  Authors
Osaki S.
  Title
Kinetic studies of ferrous ion oxidation with crystalline human ferroxidase (ceruloplasmin).
  Journal
J. Biol. Chem. 241 (1966) 5053-9.
Reference
2  [PMID:6027241]
  Authors
Osaki S, Walaas O.
  Title
Kinetic studies of ferrous ion oxidation with crystalline human ferroxidase. II. Rate constants at various steps and formation of a possible enzyme-substrate complex.
  Journal
J. Biol. Chem. 242 (1967) 2653-7.
Reference
3
  Authors
Lindley, P.F. Card, G. Zaitseva, I. Zaitsev, V. Reinhammar, B. SelinLindgren, E. and Yoshida, K.
  Title
An X-ray structural study of human ceruloplasmin in relation to ferroxidase activity.
  Journal
J. Biol. Inorg. Chem. 2 (1997) 454-463.
Reference
4  [PMID:11248684]
  Authors
Takai M, Kamimura K, Sugio T
  Title
A new iron oxidase from a moderately thermophilic iron oxidizing bacterium strain TI-1.
  Journal
Eur. J. Biochem. 268 (2001) 1653-8.
Reference
5  [PMID:14751926]
  Authors
Chen H, Attieh ZK, Su T, Syed BA, Gao H, Alaeddine RM, Fox TC, Usta J, Naylor CE, Evans RW, McKie AT, Anderson GJ, Vulpe CD
  Title
Hephaestin is a ferroxidase that maintains partial activity in sex-linked anemia  mice.
  Journal
Blood. 103 (2004) 3933-9.
  Sequence
[mmu:15203]
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
9031-37-2 104404-69-5

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