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Updated: Aug 1, 2025
09:43
Measurement of Heme Synthesis Levels in Mammalian Cells
Published on: July 9, 2015
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Functional Diversity of HemN-like Proteins.
Jinduo Cheng1, Wan-Qiu Liu1, Xiaoyu Zhu1
1Department of Chemistry, Fudan University, Shanghai, 200433, China.
ACS Bio & Med Chem Au
|April 27, 2023
Summary
HemN, a radical S-adenosylmethionine enzyme, is crucial for heme biosynthesis. HemN-like proteins, however, exhibit diverse functions beyond this role, challenging their common annotation.
Area of Science:
- Biochemistry
- Enzymology
- Molecular Biology
Background:
- HemN is a radical S-adenosylmethionine (SAM) enzyme essential for heme biosynthesis.
- It catalyzes the anaerobic oxidative decarboxylation of coproporphyrinogen III to protoporphyrinogen IX.
- HemN-like proteins are conserved across prokaryotes and eukaryotes.
Purpose of the Study:
- To review recent advances in understanding HemN-like proteins.
- To highlight the diverse functions and chemistries of this protein family.
- To address the misannotation of many HemN-like proteins in public databases.
Main Methods:
- Literature review of recent research on HemN and HemN-like proteins.
- Analysis of functional annotations and experimental data for HemN-like proteins.
- Comparative analysis of protein structures and catalytic mechanisms.
Main Results:
- HemN-like proteins are frequently misannotated as anaerobic coproporphyrinogen III oxidases (CPOs).
- This protein family encompasses diverse functions including methyltransferases, cyclopropanases, and heme chaperones.
- Recent studies reveal novel catalytic activities and biological roles for HemN-like proteins.
Conclusions:
- The HemN-like protein family is functionally diverse, extending beyond CPO activity.
- Re-evaluation of HemN-like protein annotations is necessary.
- Further research is needed to fully elucidate the diverse roles of these proteins.
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