EC 1.3.98.6     
Accepted name: AdoMet-dependent heme synthase
Reaction: Fe-coproporphyrin III + 2 S-adenosyl-L-methionine = protoheme + 2 CO2 + 2 5′-deoxyadenosine + 2 L-methionine
Other name(s): ahbD (gene name); SAM-dependent heme synthase
Systematic name: Fe-coproporphyrin III:S-adenosyl-L-methionine oxidoreductase (decarboxylating)
Comments: This radical AdoMet enzyme participates in a heme biosynthesis pathway found in archaea and sulfur-reducing bacteria. cf. EC 1.3.98.5, hydrogen peroxide-dependent heme synthase.
References:
1.  Bali, S., Lawrence, A.D., Lobo, S.A., Saraiva, L.M., Golding, B.T., Palmer, D.J., Howard, M.J., Ferguson, S.J. and Warren, M.J. Molecular hijacking of siroheme for the synthesis of heme and d1 heme. Proc. Natl. Acad. Sci. USA 108 (2011) 18260–18265. [PMID: 21969545]
2.  Kuhner, M., Haufschildt, K., Neumann, A., Storbeck, S., Streif, J. and Layer, G. The alternative route to heme in the methanogenic archaeon Methanosarcina barkeri. Archaea 2014:327637 (2014). [PMID: 24669201]
[EC 1.3.98.6 created 2019]
 
 


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