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Redefining the role of the EryM acetyltransferase in natural product biosynthetic pathways
Open accessPublished version of a preprint
Abstract
The GNAT (GCN5-related N-acetyltransferase) superfamily comprises enzymes with a conserved fold and diverse catalytic activities, including primarily acyl transfer, with a few examples of decarboxylation. EryM, a GNAT from Saccharopolyspora erythraea, has been implicated in both erythromycin and erythrochelin biosynthesis, with dual functionality as an acetyltransferase and a decarboxylase. Despite an historical association with malonyl-coenzyme A decarboxylation activity, this dual activity has remained enigmatic as its close homologs were identified with only acyl transfer activity. Here, functional assays demonstrate that EryM catalyzes acyl transfer but lacks decarboxylation activity, challenging long-standing assumptions about its biosynthetic role. Crystal structures of EryM and an acetyl-CoA complex and comparison with homologs in siderophore pathways reveal a conserved catalytic pocket with an essential His and identically positioned side chains common to GNAT enzymes for N-acyl transfer from CoA to primary hydroxylamine substrates. Bioinformatic analysis defines a large GNAT subfamily broadly distributed in the microbial world.
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Research works printed but not linked: 1
- New ClusteredNR database: faster searches and more informative BLAST results - NCBI Insights https://ncbiinsights.ncbi.nlm.nih.gov/2022/05/02/clusterednr_1/.
Metadata
- Authors
- Li, Y., Liu, X., Harris, N. R., Roberts, J. R., Valdivia, E. M., Ji, X., & Smith, J. L.
- Affiliations
- University of Michigan (US)
- Corresponding author
- Smith, Janet L.
- Venue
- Structure
- Publisher
- Elsevier BV
- Published
- 2025-08
- Volume
- 33
- Issue
- 8
- Pages
- 1352-1361.e3
- ISSN
- 0969-2126 (ISSN-L)
- PMC
- PMC12335365
- OpenAlex
- W4411257025
- Cited by
- 0
- References
- 56
- FWCI
- 0.00
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
- www.elsevier.com/open-access/userlicense/1.0/ (am, 371 d)
- doi.org/10.15223/policy-017 (stm-asf)
- doi.org/10.15223/policy-037 (stm-asf)
- doi.org/10.15223/policy-012 (stm-asf)
- doi.org/10.15223/policy-029 (stm-asf)
- doi.org/10.15223/policy-004 (stm-asf)
- Locations
- Structure (acceptedVersion)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion)
- PubMed (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed Central (submittedVersion)
- Funders
- National Institutes of Health National Cancer Institute (ACB-12002)
- National Institutes of Health (R01 DK042303)
- Life Sciences, University of California, Los Angeles (P30 GM138396)
- Topics
- Life Sciences › Immunology and Microbiology › Applied Microbiology and Biotechnology › Microbial Natural Products and Biosynthesis
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biotechnology › Microbial Metabolism and Applications
- Keywords
- GNAT superfamily, N-acetyltransferase, acyl transfer, decarboxylation, erythromycin biosynthesis, Saccharopolyspora erythraea, acetyl-CoA, crystal structure, catalytic pocket, siderophore biosynthesis, natural product biosynthesis
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- CoChat. (2026). Citation check: Redefining the role of the EryM acetyltransferase in natural product biosynthetic pathways. https://app.cochat.ai/papers/10.1016/j.str.2025.05.011
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- Li, Y., Liu, X., Harris, N. R., Roberts, J. R., Valdivia, E. M., Ji, X., & Smith, J. L. (2025). Redefining the role of the EryM acetyltransferase in natural product biosynthetic pathways. Structure. https://doi.org/10.1016/j.str.2025.05.011
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