| Structural highlights
Function
CHDC_LISMO Involved in coproporphyrin-dependent heme b biosynthesis (PubMed:27758026, PubMed:31423350). Catalyzes the decarboxylation of Fe-coproporphyrin III (coproheme) to heme b (protoheme IX), the last step of the pathway (PubMed:27758026, PubMed:29536725, PubMed:31423350). The reaction occurs in a stepwise manner with a three-propionate intermediate (PubMed:27758026, PubMed:31423350).[1] [2] [3]
References
- ↑ Hofbauer S, Mlynek G, Milazzo L, Puhringer D, Maresch D, Schaffner I, Furtmuller PG, Smulevich G, Djinovic-Carugo K, Obinger C. Hydrogen peroxide-mediated conversion of coproheme to heme b by HemQ - Lessons from the first crystal structure and kinetic studies. FEBS J. 2016 Oct 18. doi: 10.1111/febs.13930. PMID:27758026 doi:https://dx.doi.org/10.1111/febs.13930
- ↑ Milazzo L, Hofbauer S, Howes BD, Gabler T, Furtmüller PG, Obinger C, Smulevich G. Insights into the Active Site of Coproheme Decarboxylase from Listeria monocytogenes. Biochemistry. 2018 Apr 3;57(13):2044-2057. PMID:29536725 doi:10.1021/acs.biochem.8b00186
- ↑ Milazzo L, Gabler T, Puhringer D, Jandova Z, Maresch D, Michlits H, Pfanzagl V, Djinovic-Carugo K, Oostenbrink C, Furtmuller PG, Obinger C, Smulevich G, Hofbauer S. Redox Cofactor Rotates during Its Stepwise Decarboxylation: Molecular Mechanism of Conversion of Coproheme to Heme b. ACS Catal. 2019 Aug 2;9(8):6766-6782. doi: 10.1021/acscatal.9b00963. Epub 2019, Jun 18. PMID:31423350 doi:https://dx.doi.org/10.1021/acscatal.9b00963
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