Revisiting the Mechanism of the Anaerobic Coproporphyrinogen III Oxidase HemN

Ji, Xinjian; Mo, Tianlu; Liu, Wanqiu; Ding, Wei; Deng, Zixin; Zhang, Qi

doi:10.1002/ange.201814708

Cited by 9 publications

(1 citation statement)

References 53 publications

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“…The existence of the methylene radical 28 during the catalysis was supported by the observation of a conjugate of SAM and the mono-decarboxylated product. Subsequently, the methylene radical species 28 abstracts a hydrogen atom from the β-carbon of the propionate group of coproporphyrinogen III ( 16 ), which may be followed by decarboxylation involving a single electron transfer to the [Fe 4 S 4 ] 2+ cluster (Ji et al, 2019 ) ( Fig. 3C ).…”

Section: Hemf Hemn and Hemq In The Biosynthesis Of Heme Bmentioning

confidence: 99%

Diverse enzymatic chemistry for propionate side chain cleavages in tetrapyrrole biosynthesis

Ushimaru

Lyu

Abe

2023

Journal of Industrial Microbiology and Biotechnology

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Tetrapyrroles represent a unique class of natural products that possess diverse chemical architectures and exhibit a broad range of biological functions. Accordingly, they attract keen attention from the natural product community. Many metal-chelating tetrapyrroles serve as enzyme cofactors essential for life, while certain organisms produce metal-free porphyrin metabolites with biological activities potentially beneficial for the producing organisms and for human use. The unique properties of tetrapyrrole natural products derive from their extensively modified and highly conjugated macrocyclic core structures. Most of these various tetrapyrrole natural products biosynthetically originate from a branching point precursor, uroporphyrinogen III, which contains propionate and acetate side chains on its macrocycle. Over the past few decades, many modification enzymes with unique catalytic activities, and the diverse enzymatic chemistries employed to cleave the propionate side chains from the macrocycles, have been identified. In this review, we highlight the tetrapyrrole biosynthetic enzymes required for the propionate side chain removal processes and discuss their various chemical mechanisms.

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Section: Hemf Hemn and Hemq In The Biosynthesis Of Heme Bmentioning

confidence: 99%

Diverse enzymatic chemistry for propionate side chain cleavages in tetrapyrrole biosynthesis

Ushimaru

Lyu

Abe

2023

Journal of Industrial Microbiology and Biotechnology

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Sulfonium‐Based Homolytic Substitution Observed for the Radical SAM Enzyme HemN

Mandalapu

et al. 2020

Angewandte Chemie

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Characterization and Mechanistic Study of the Radical SAM Enzyme ArsS Involved in Arsenosugar Biosynthesis

Cheng

et al. 2021

Angewandte Chemie

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Arsenosugars are a group of arsenic‐containing ribosides that are found predominantly in marine algae but also in terrestrial organisms. It has been proposed that arsenosugar biosynthesis involves a key intermediate 5′‐deoxy‐5′‐dimethylarsinoyl‐adenosine (DDMAA), but how DDMAA is produced remains elusive. Now, we report characterization of ArsS as a DDMAA synthase, which catalyzes a radical S‐adenosylmethionine (SAM)‐mediated alkylation (adenosylation) of dimethylarsenite (DMAsIII) to produce DDMAA. This radical‐mediated reaction is redox neutral, and multiple turnover can be achieved without external reductant. Phylogenomic and biochemical analyses revealed that DDMAA synthases are widespread in distinct bacterial phyla with similar catalytic efficiencies; these enzymes likely originated from cyanobacteria. This study reveals a key step in arsenosugar biosynthesis and also a new paradigm in radical SAM chemistry, highlighting the catalytic diversity of this superfamily of enzymes.

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Revisiting the Mechanism of the Anaerobic Coproporphyrinogen III Oxidase HemN

Abstract: Supportinginformation and the ORCID identification number(s) for the author(s) of this article can be found under: https://doi.

Cited by 9 publications

References 53 publications

Diverse enzymatic chemistry for propionate side chain cleavages in tetrapyrrole biosynthesis

Diverse enzymatic chemistry for propionate side chain cleavages in tetrapyrrole biosynthesis

Sulfonium‐Based Homolytic Substitution Observed for the Radical SAM Enzyme HemN

Characterization and Mechanistic Study of the Radical SAM Enzyme ArsS Involved in Arsenosugar Biosynthesis

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