Discovery of a New Class of Aminoacyl Radical Enzymes Expands Nature’s Known Radical Chemistry
Radical enzymes, including the evolutionarily ancient glycyl radical enzyme (GRE) family, catalyze chemically challenging reactions that are involved in a myriad of important biological processes. All GREs possess an essential, conserved backbone glycine that forms a stable, catalytically essential...
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| Published in | Journal of the American Chemical Society Vol. 146; no. 43; pp. 29645 - 29655 |
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| Main Authors | , , , , , , , , |
| Format | Journal Article |
| Language | English |
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United States
American Chemical Society
30.10.2024
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| Abstract | Radical enzymes, including the evolutionarily ancient glycyl radical enzyme (GRE) family, catalyze chemically challenging reactions that are involved in a myriad of important biological processes. All GREs possess an essential, conserved backbone glycine that forms a stable, catalytically essential α-carbon radical. Through close examination of the GRE family, we unexpectedly identified hundreds of noncanonical GRE homologs that encode either an alanine, serine, or threonine in place of the catalytic glycine residue. Contrary to a long-standing belief, we experimentally demonstrate that these aminoacyl radical enzymes (AAREs) form stable α-carbon radicals on the three cognate residues when activated by partner activating enzymes. The previously unrecognized AAREs are widespread in microbial genomes, highlighting their biological importance and potential for exhibiting new reactivity. Collectively, these studies expand the known radical chemistry of living systems while raising questions about the evolutionary emergence of the AAREs. |
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| AbstractList | Radical enzymes, including the evolutionarily ancient glycyl radical enzyme (GRE) family, catalyze chemically challenging reactions that are involved in a myriad of important biological processes. All GREs possess an essential, conserved backbone glycine that forms a stable, catalytically essential α-carbon radical. Through close examination of the GRE family, we unexpectedly identified hundreds of noncanonical GRE homologs that encode either an alanine, serine, or threonine in place of the catalytic glycine residue. Contrary to a long-standing belief, we experimentally demonstrate that these aminoacyl radical enzymes (AAREs) form stable α-carbon radicals on the three cognate residues when activated by partner activating enzymes. The previously unrecognized AAREs are widespread in microbial genomes, highlighting their biological importance and potential for exhibiting new reactivity. Collectively, these studies expand the known radical chemistry of living systems while raising questions about the evolutionary emergence of the AAREs. Radical enzymes, including the evolutionarily ancient glycyl radical enzyme (GRE) family, catalyze chemically challenging reactions that are involved in a myriad of important biological processes. All GREs possess an essential, conserved backbone glycine that forms a stable, catalytically essential α-carbon radical. Through close examination of the GRE family, we unexpectedly identified hundreds of noncanonical GRE homologs that encode either an alanine, serine, or threonine in place of the catalytic glycine residue. Contrary to a long-standing belief, we experimentally demonstrate that these aminoacyl radical enzymes (AAREs) form stable α-carbon radicals on the three cognate residues when activated by partner activating enzymes. The previously unrecognized AAREs are widespread in microbial genomes, highlighting their biological importance and potential for exhibiting new reactivity. Collectively, these studies expand the known radical chemistry of living systems while raising questions about the evolutionary emergence of the AAREs. Radical enzymes, including the evolutionarily ancient glycyl radical enzyme (GRE) family, catalyze chemically challenging reactions that are involved in a myriad of important biological processes. All GREs possess an essential, conserved backbone glycine that forms a stable, catalytically essential α-carbon radical. Through close examination of the GRE family, we unexpectedly identified hundreds of noncanonical GRE homologs that encode either an alanine, serine, or threonine in place of the catalytic glycine residue. Contrary to a long-standing belief, we experimentally demonstrate that these aminoacyl radical enzymes (AAREs) form stable α-carbon radicals on the three cognate residues when activated by partner activating enzymes. The previously unrecognized AAREs are widespread in microbial genomes, highlighting their biological importance and potential for exhibiting new reactivity. Collectively, these studies expand the known radical chemistry of living systems while raising questions about the evolutionary emergence of the AAREs.Radical enzymes, including the evolutionarily ancient glycyl radical enzyme (GRE) family, catalyze chemically challenging reactions that are involved in a myriad of important biological processes. All GREs possess an essential, conserved backbone glycine that forms a stable, catalytically essential α-carbon radical. Through close examination of the GRE family, we unexpectedly identified hundreds of noncanonical GRE homologs that encode either an alanine, serine, or threonine in place of the catalytic glycine residue. Contrary to a long-standing belief, we experimentally demonstrate that these aminoacyl radical enzymes (AAREs) form stable α-carbon radicals on the three cognate residues when activated by partner activating enzymes. The previously unrecognized AAREs are widespread in microbial genomes, highlighting their biological importance and potential for exhibiting new reactivity. Collectively, these studies expand the known radical chemistry of living systems while raising questions about the evolutionary emergence of the AAREs. |
| Author | Broderick, William E. Hoffman, Brian H. Kountz, Duncan J. Beller, Harry R. Balskus, Emily P. Yang, Hao Lundahl, Maike N. Fu, Beverly Broderick, Joan B. |
| AuthorAffiliation | Department of Chemistry Department of Chemistry and Biochemistry Howard Hughes Medical Institute Department of Chemistry and Chemical Biology University of Toronto Department of Chemical Engineering and Applied Chemistry |
| AuthorAffiliation_xml | – name: Department of Chemical Engineering and Applied Chemistry – name: Howard Hughes Medical Institute – name: Department of Chemistry and Chemical Biology – name: Department of Chemistry – name: University of Toronto – name: Department of Chemistry and Biochemistry |
| Author_xml | – sequence: 1 givenname: Beverly orcidid: 0000-0002-2345-6911 surname: Fu fullname: Fu, Beverly organization: Department of Chemistry and Chemical Biology – sequence: 2 givenname: Hao orcidid: 0000-0001-7229-0957 surname: Yang fullname: Yang, Hao organization: Department of Chemistry – sequence: 3 givenname: Duncan J. surname: Kountz fullname: Kountz, Duncan J. organization: Department of Chemistry and Chemical Biology – sequence: 4 givenname: Maike N. orcidid: 0000-0002-4391-7279 surname: Lundahl fullname: Lundahl, Maike N. organization: Department of Chemistry and Biochemistry – sequence: 5 givenname: Harry R. orcidid: 0000-0001-9637-3650 surname: Beller fullname: Beller, Harry R. organization: University of Toronto – sequence: 6 givenname: William E. orcidid: 0000-0001-5782-7322 surname: Broderick fullname: Broderick, William E. organization: Department of Chemistry and Biochemistry – sequence: 7 givenname: Joan B. surname: Broderick fullname: Broderick, Joan B. organization: Department of Chemistry and Biochemistry – sequence: 8 givenname: Brian H. orcidid: 0000-0002-3100-0746 surname: Hoffman fullname: Hoffman, Brian H. organization: Department of Chemistry – sequence: 9 givenname: Emily P. orcidid: 0000-0001-5985-5714 surname: Balskus fullname: Balskus, Emily P. email: balskus@chemistry.harvard.edu organization: Howard Hughes Medical Institute |
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| Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 This paper originally published ASAP on October 11, 2024. Several text corrections were made throughout the paper and a new version reposted on October 14, 2024. |
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| Title | Discovery of a New Class of Aminoacyl Radical Enzymes Expands Nature’s Known Radical Chemistry |
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