The Molecular Evolution, Structure, and Function of Coproporphyrinogen Oxidase and Protoporphyrinogen Oxidase in Prokaryotes
Coproporphyrinogen oxidase (CgoX) and protoporphyrinogen oxidase (PgoX) catalyze the oxidation of the flexible cyclic tetrapyrrole of porphyrinogen compounds into fully conjugated, planar macrocyclic porphyrin compounds during heme biosynthesis. These enzymes are activated via different pathways. Cg...
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2023-12-01
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| author | Marcel Zámocký Stefan Hofbauer Thomas Gabler Paul G. Furtmüller |
| author_facet | Marcel Zámocký Stefan Hofbauer Thomas Gabler Paul G. Furtmüller |
| author_sort | Marcel Zámocký |
| collection | DOAJ |
| description | Coproporphyrinogen oxidase (CgoX) and protoporphyrinogen oxidase (PgoX) catalyze the oxidation of the flexible cyclic tetrapyrrole of porphyrinogen compounds into fully conjugated, planar macrocyclic porphyrin compounds during heme biosynthesis. These enzymes are activated via different pathways. CgoX oxidizes coproporphyrinogen III to coproporphyrin III in the coproporphyrin-dependent pathway, whereas PgoX oxidizes protoporphyrinogen IX to protoporphyrin IX in the penultimate step of the protoporphyrin-dependent pathway. The phylogenetic analysis presented herein demonstrates a clear differentiation between the two enzyme classes, as evidenced by the clustering of sequences in distinct clades, and it shows that, at the origin of porphyrinogen-type oxidase evolution, PgoXs from cyanobacteria were found, which were noticeably separated from descendant PgoX representatives of <i>Deltaproteobacteria</i> and all later PgoX variants, leading to many eukaryotic clades. CgoX sequences originating from the monoderm <i>Actinomycetota</i> and <i>Bacillota</i> were well separated from the predecessor clades containing PgoX types and represent a peculiar type of gene speciation. The structural similarities and differences between these two oxidases are discussed based on their protein sequence alignment and a structural comparison. |
| first_indexed | 2024-03-08T20:59:12Z |
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| issn | 2079-7737 |
| language | English |
| last_indexed | 2024-03-08T20:59:12Z |
| publishDate | 2023-12-01 |
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| spelling | doaj.art-eff91766a6a64e459c2ac5fb67d6e5f12023-12-22T13:54:33ZengMDPI AGBiology2079-77372023-12-011212152710.3390/biology12121527The Molecular Evolution, Structure, and Function of Coproporphyrinogen Oxidase and Protoporphyrinogen Oxidase in ProkaryotesMarcel Zámocký0Stefan Hofbauer1Thomas Gabler2Paul G. Furtmüller3Laboratory of Phylogenomic Ecology, Institute of Molecular Biology, Slovak Academy of Sciences, Dúbravská Cesta 21, SK-84551 Bratislava, SlovakiaInstitute of Biochemistry, Department of Chemistry, University of Natural Resources and Life Sciences, Vienna, Muthgasse 18, A-1190 Vienna, AustriaInstitute of Biochemistry, Department of Chemistry, University of Natural Resources and Life Sciences, Vienna, Muthgasse 18, A-1190 Vienna, AustriaInstitute of Biochemistry, Department of Chemistry, University of Natural Resources and Life Sciences, Vienna, Muthgasse 18, A-1190 Vienna, AustriaCoproporphyrinogen oxidase (CgoX) and protoporphyrinogen oxidase (PgoX) catalyze the oxidation of the flexible cyclic tetrapyrrole of porphyrinogen compounds into fully conjugated, planar macrocyclic porphyrin compounds during heme biosynthesis. These enzymes are activated via different pathways. CgoX oxidizes coproporphyrinogen III to coproporphyrin III in the coproporphyrin-dependent pathway, whereas PgoX oxidizes protoporphyrinogen IX to protoporphyrin IX in the penultimate step of the protoporphyrin-dependent pathway. The phylogenetic analysis presented herein demonstrates a clear differentiation between the two enzyme classes, as evidenced by the clustering of sequences in distinct clades, and it shows that, at the origin of porphyrinogen-type oxidase evolution, PgoXs from cyanobacteria were found, which were noticeably separated from descendant PgoX representatives of <i>Deltaproteobacteria</i> and all later PgoX variants, leading to many eukaryotic clades. CgoX sequences originating from the monoderm <i>Actinomycetota</i> and <i>Bacillota</i> were well separated from the predecessor clades containing PgoX types and represent a peculiar type of gene speciation. The structural similarities and differences between these two oxidases are discussed based on their protein sequence alignment and a structural comparison.https://www.mdpi.com/2079-7737/12/12/1527phylogenetic analysissequence alignmentprokaryotic heme biosynthesiscoproporphyrin-dependent pathwayprotoporphyrin-dependent pathwaycoproporphyrinogen III oxidase |
| spellingShingle | Marcel Zámocký Stefan Hofbauer Thomas Gabler Paul G. Furtmüller The Molecular Evolution, Structure, and Function of Coproporphyrinogen Oxidase and Protoporphyrinogen Oxidase in Prokaryotes Biology phylogenetic analysis sequence alignment prokaryotic heme biosynthesis coproporphyrin-dependent pathway protoporphyrin-dependent pathway coproporphyrinogen III oxidase |
| title | The Molecular Evolution, Structure, and Function of Coproporphyrinogen Oxidase and Protoporphyrinogen Oxidase in Prokaryotes |
| title_full | The Molecular Evolution, Structure, and Function of Coproporphyrinogen Oxidase and Protoporphyrinogen Oxidase in Prokaryotes |
| title_fullStr | The Molecular Evolution, Structure, and Function of Coproporphyrinogen Oxidase and Protoporphyrinogen Oxidase in Prokaryotes |
| title_full_unstemmed | The Molecular Evolution, Structure, and Function of Coproporphyrinogen Oxidase and Protoporphyrinogen Oxidase in Prokaryotes |
| title_short | The Molecular Evolution, Structure, and Function of Coproporphyrinogen Oxidase and Protoporphyrinogen Oxidase in Prokaryotes |
| title_sort | molecular evolution structure and function of coproporphyrinogen oxidase and protoporphyrinogen oxidase in prokaryotes |
| topic | phylogenetic analysis sequence alignment prokaryotic heme biosynthesis coproporphyrin-dependent pathway protoporphyrin-dependent pathway coproporphyrinogen III oxidase |
| url | https://www.mdpi.com/2079-7737/12/12/1527 |
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