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Ferrochelatase
From Proteopedia
(Difference between revisions)
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<StructureSection load='1c1h' size='350' side='right' scene='' caption='Ferrochelatase with methylmesoporphyrin and Mg+2 ion (PDB code [[1c1h]])'> | <StructureSection load='1c1h' size='350' side='right' scene='' caption='Ferrochelatase with methylmesoporphyrin and Mg+2 ion (PDB code [[1c1h]])'> | ||
| + | == Function == | ||
| - | '''Ferrochelatase''' (FECH) catalyzes the last step in the formation of heme. FECH adds Fe+2 to protoporphyrin IX converting it to protoheme. The human FECH is a homodimer containing 2 similar domains and an iron-sulfur cluster. Defective FECH is the cause of porphyria. | + | '''Ferrochelatase''' (FECH) catalyzes the last step in the formation of heme. FECH adds Fe+2 to protoporphyrin IX converting it to protoheme. The human FECH is a homodimer containing 2 similar domains and an iron-sulfur cluster. |
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| + | == Disease == | ||
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| + | Defective FECH is the cause of porphyria<ref>PMID 11929052</ref>. | ||
'''Bacterial ferrochelatase turns human: Tyr13 determines the apparent metal specificity of ''Bacillus subtilis'' ferrochelatase <ref>DOI 10.1007/s00775-010-0720-4</ref>''' | '''Bacterial ferrochelatase turns human: Tyr13 determines the apparent metal specificity of ''Bacillus subtilis'' ferrochelatase <ref>DOI 10.1007/s00775-010-0720-4</ref>''' | ||
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**[[1c9e]] - BsFECH + N-methylmesoporphyrin + Cu + Mg<br /> | **[[1c9e]] - BsFECH + N-methylmesoporphyrin + Cu + Mg<br /> | ||
}} | }} | ||
| - | + | == References == | |
<references/> | <references/> | ||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Revision as of 08:50, 2 March 2016
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3D structures of ferrochelatase
Updated on 02-March-2016
References
- ↑ Chen FP, Risheg H, Liu Y, Bloomer J. Ferrochelatase gene mutations in erythropoietic protoporphyria: focus on liver disease. Cell Mol Biol (Noisy-le-grand). 2002 Feb;48(1):83-9. PMID:11929052
- ↑ Hansson MD, Karlberg T, Soderberg CA, Rajan S, Warren MJ, Al-Karadaghi S, Rigby SE, Hansson M. Bacterial ferrochelatase turns human: Tyr13 determines the apparent metal specificity of Bacillus subtilis ferrochelatase. J Biol Inorg Chem. 2010 Nov 4. PMID:21052751 doi:10.1007/s00775-010-0720-4
