7q4f
Structure of coproheme decarboxylase from Corynebacterium dipththeriae W183Y mutant in complex with coprohemeStructure of coproheme decarboxylase from Corynebacterium dipththeriae W183Y mutant in complex with coproheme
Structural highlights
FunctionQ6NGV6_CORDI Involved in coproporphyrin-dependent heme b biosynthesis. Catalyzes the decarboxylation of Fe-coproporphyrin III (coproheme) to heme b (protoheme IX), the last step of the pathway. The reaction occurs in a stepwise manner with a three-propionate intermediate.[HAMAP-Rule:MF_02244] Publication Abstract from PubMedThe oxidative decarboxylation of coproheme to form heme b by coproheme decarboxylase is a stereospecific two-step reaction. In the first step, the propionate at position two (p2) is cleaved off the pyrrole ring A to form a vinyl group at this position. Subsequently, the propionate at position four (p4) on pyrrole ring B is cleaved off and heme b is formed. In this study, we attempted to engineer coproheme decarboxylase from Corynebacterium diphtheriae to alter the stereospecificity of this reaction. By introducing a tyrosine residue in proximity to the propionate at position 4, we were able to create a new radical center in the active site. However, the artificial Tyr183(*) radical could not be shown to catalyze any decarboxylation. Initial Steps to Engineer Coproheme Decarboxylase to Obtain Stereospecific Monovinyl, Monopropionyl Deuterohemes.,Michlits H, Valente N, Mlynek G, Hofbauer S Front Bioeng Biotechnol. 2022 Jan 24;9:807678. doi: 10.3389/fbioe.2021.807678., eCollection 2021. PMID:35141216[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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