EC 1.16.3.2 - Bacterial non-heme ferritin

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IntEnz Enzyme Nomenclature
EC 1.16.3.2

Names

Accepted name:
bacterial non-heme ferritin
Other names:
FtnA
HuHF
Systematic name:
Fe(II):oxygen oxidoreductase ([FeO(OH)]core-producing)

Reactions

Comments:

Ferritins are intracellular iron-storage and detoxification proteins found in all kingdoms of life. They are formed from two subunits that co-assemble in various ratios to form a spherical protein shell. Thousands of mineralized iron atoms are stored within the core of the structure. The product of dioxygen reduction by the bacterial non-heme ferritin is hydrogen peroxide, which is consumed in a subsequent reaction.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
UniProtKB/Swiss-Prot: (23) [show] [UniProt]

References

  1. Hudson, A. J., Andrews, S. C., Hawkins, C., Williams, J. M., Izuhara, M., Meldrum, F. C., Mann, S., Harrison, P. M., Guest, J. R.
    Overproduction, purification and characterization of the Escherichia coli ferritin.
    Eur. J. Biochem. 218: 985-995 (1993). [PMID: 8281950]
  2. Stillman, T. J., Hempstead, P. D., Artymiuk, P. J., Andrews, S. C., Hudson, A. J., Treffry, A., Guest, J. R., Harrison, P. M.
    The high-resolution X-ray crystallographic structure of the ferritin (EcFtnA) of Escherichia coli; comparison with human H ferritin (HuHF) and the structures of the Fe(3+) and Zn(2+) derivatives.
    J. Mol. Biol. 307: 587-603 (2001). [PMID: 11254384]
  3. Bou-Abdallah, F., Yang, H., Awomolo, A., Cooper, B., Woodhall, M. R., Andrews, S. C., Chasteen, N. D.
    Functionality of the three-site ferroxidase center of Escherichia coli bacterial ferritin (EcFtnA).
    Biochemistry 53: 483-495 (2014). [PMID: 24380371]

[EC 1.16.3.2 created 2014]