ExplorEnz: EC 4.99.1.9

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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, PDB

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. [DOI] [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. [DOI] [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. [DOI] [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. [DOI] [PMID: 25646457]

[EC 4.99.1.9 created 2016]