Member database | PROSITE patterns |
PROSITE patterns type | conserved site |
Short name | FERROCHELATASE |
Description
Ferrochelatase (EC 4.99.1.1) (protoheme ferro-lyase)
[2] catalyzes the last
step in heme biosynthesis: the chelation of a ferrous ion to proto-porphyrin
IX, to form protoheme.
In eukaryotes, ferrochelatase is a mitochondrial protein bound to the inner
membrane, whose active site faces the mitochondrial matrix. The mature form of
eukaryotic ferrochelatase is composed of about 360 amino acids. In bacteria,
ferrochelatase (gene hemH)
[1] is a protein of from 310 to 380 amino acids.
The human autosomal dominant disease protoporphyria is due to the reduced
activity of ferrochelatase.
The signature pattern for this enzyme is based on a conserved region which
contains a histidine residue which could be involved in binding iron.
References
1.Isolation and characterization of visible light-sensitive mutants of Escherichia coli K12. Miyamoto K, Nakahigashi K, Nishimura K, Inokuchi H. J. Mol. Biol. 219, 393-8, (1991). View articlePMID: 2051480
2.Cloning of murine ferrochelatase. Brenner DA, Frasier F. Proc. Natl. Acad. Sci. U.S.A. 88, 849-53, (1991). View articlePMID: 1704134