The Enzyme Database

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EC 4.99.1.9     
Accepted name: coproporphyrin ferrochelatase
Reaction: Fe-coproporphyrin III + 2 H+ = coproporphyrin III + Fe2+
Glossary: Fe-coproporphyrin III = coproheme III
Other name(s): hemH (gene name)
Systematic name: protoheme ferro-lyase (protoporphyrin-forming)
Comments: The enzyme, present in Gram-positive bacteria, participates in heme biosynthesis. It can also catalyse the reaction of EC 4.99.1.1, protoporphyrin IX ferrochelatase, at a much lower level.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Hansson, M. and Hederstedt, L. Purification and characterisation of a water-soluble ferrochelatase from Bacillus subtilis. Eur. J. Biochem. 220 (1994) 201–208. [PMID: 8119288]
2.  Al-Karadaghi, S., Hansson, M., Nikonov, S., Jonsson, B. and Hederstedt, L. Crystal structure of ferrochelatase: the terminal enzyme in heme biosynthesis. Structure 5 (1997) 1501–1510. [PMID: 9384565]
3.  Hansson, M.D., Karlberg, T., Soderberg, C.A., Rajan, S., Warren, M.J., Al-Karadaghi, S., Rigby, S.E. and Hansson, M. Bacterial ferrochelatase turns human: Tyr13 determines the apparent metal specificity of Bacillus subtilis ferrochelatase. J. Biol. Inorg. Chem. 16 (2011) 235–242. [PMID: 21052751]
4.  Dailey, H.A., Gerdes, S., Dailey, T.A., Burch, J.S. and Phillips, J.D. Noncanonical coproporphyrin-dependent bacterial heme biosynthesis pathway that does not use protoporphyrin. Proc. Natl. Acad. Sci. USA 112 (2015) 2210–2215. [PMID: 25646457]
[EC 4.99.1.9 created 2016]
 
 


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