IntEnz

EC 1.16.3.1 - Ferroxidase

IntEnz Enzyme Nomenclature
EC 1.16.3.1

Names

Reaction

• 11148 [IUBMB]
  4

  Fe²⁺

  Fe(2+)

  Name origin: UniProt - CHECKED (C)

  CHEBI:29033

  Formula: Fe
  Charge: 2

  ChEBI compound status: CHECKED (C)

  

  +

  4

  H⁺

  H(+)

  Name origin: UniProt - CHECKED (C)

  CHEBI:15378

  Formula: H
  Charge: 1

  ChEBI compound status: CHECKED (C)

  

  +

  O₂

  O2

  Name origin: UniProt - CHECKED (C)

  CHEBI:15379

  Formula: O2
  Charge: 0

  ChEBI compound status: CHECKED (C)

  

  =

  4

  Fe³⁺

  Fe(3+)

  Name origin: UniProt - CHECKED (C)

  CHEBI:29034

  Formula: Fe
  Charge: 3

  ChEBI compound status: CHECKED (C)

  

  +

  2

  H₂O

  H2O

  Name origin: UniProt - CHECKED (C)

  CHEBI:15377

  Formula: H2O
  Charge: 0

  ChEBI compound status: CHECKED (C)

  

Cofactor

• Cu cation

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.

Links to other databases

References

1. Osaki, S.
   Kinetic studies of ferrous ion oxidation with crystalline human ferroxidase (ceruloplasmin).
   J. Biol. Chem. 241: 5053-5059 (1966). [PMID: 5925868]
2. Osaki, S. and Walaas, O.
   Kinetic studies of ferrous ion oxidation with crystalline human ferroxidase. II. Rate constants at various steps and formation of a possible enzyme-substrate complex.
   J. Biol. Chem. 242: 2653-2657 (1967). [PMID: 6027241]
3. Lindley, P.F. Card, G. Zaitseva, I. Zaitsev, V. Reinhammar, B. SelinLindgren, E. and Yoshida, K.
   An X-ray structural study of human ceruloplasmin in relation to ferroxidase activity.
   J. Biol. Inorg. Chem. 2: 454-463 (1997).
4. Takai, M., Kamimura, K., Sugio, T.
   A new iron oxidase from a moderately thermophilic iron oxidizing bacterium strain TI-1.
   Eur. J. Biochem. 268: 1653-1658 (2001). [PMID: 11248684]
5. Chen, H., Attieh, Z. K., Su, T., Syed, B. A., Gao, H., Alaeddine, R. M., Fox, T. C., Usta, J., Naylor, C. E., Evans, R. W., McKie, A. T., Anderson, G. J., Vulpe, C. D.
   Hephaestin is a ferroxidase that maintains partial activity in sex-linked anemia mice.
   Blood 103: 3933-3939 (2004). [PMID: 14751926]

[EC 1.16.3.1 created 1972, modified 2011]