ArticleeLife2021
Structure and mechanism of a phage-encoded SAM lyase revises catalytic function of enzyme family.
Article in eLife, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- Isolation and genomic characterization of a Teetrevirus phage infecting Klebsiella quasipneumoniae with a putative SAMase gene.Archives of virology · 2026Article
- Isolation and genomic characterization of a Teetrevirus phage infecting Klebsiella quasipneumoniae with a putative SAMase gene.Archives of virology · 2026Article
- Molecular basis of SAM-AMP synthesis and degradation in the type III-B CRISPR-Cas system.Nature chemical biology · 2026Article
- Bacteriophage lysins: a promising strategy for combating foodborne pathogens in food safety.Frontiers in microbiology · 2026Review
- Genomic, Functional, and Evolutionary Insights into a Novel T7-like Phage B1 Infecting Multidrug-ResistantInternational journal of molecular sciences · 2025Article
- Biology of host-dependent restriction-modification in prokaryotes.EcoSal Plus · 2025Review
- SAM-AMP lyases in type III CRISPR defence.Nucleic acids research · 2025Article
- Two virulent Vibrio campbellii phages with potential for phage therapy in aquaculture.BMC microbiology · 2025Article
- Molecular basis for azetidine-2-carboxylic acid biosynthesis.Nature communications · 2025Article
- Isolation and characterization of 24 phages infecting the plant growth-promoting rhizobacterium Klebsiella sp. M5al.PloS one · 2025Article
- Phylogeny and disease associations of a widespread and ancient intestinal bacteriophage lineage.Nature communications · 2024Article
- RecA-dependent or independent recombination of plasmid DNA generates a conflict with the host EcoKI immunity by launching restriction alleviation.Nucleic acids research · 2024Article
- Increased mutations in lipopolysaccharide biosynthetic genes cause time-dependent development of phage resistance inAntimicrobial agents and chemotherapy · 2024Article
- het-B allorecognition in Podospora anserina is determined by pseudo-allelic interaction of genes encoding a HET and lectin fold domain protein and a PII-like protein.PLoS genetics · 2024Article
- Functionally comparable but evolutionarily distinct nucleotide-targeting effectors help identify conserved paradigms across diverse immune systems.Nucleic acids research · 2023Article
- Article
- Synergistic action of phages and lytic proteins with antibiotics: a combination strategy to target bacteria and biofilms.BMC microbiology · 2023Article
- A novel long-tailed myovirus represents a new T4-like cyanophage cluster.Frontiers in microbiology · 2023Article
- Article
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Authors and funding
12 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The first S-adenosyl methionine (SAM) degrading enzyme (SAMase) was discovered in bacteriophage T3, as a counter-defense against the bacterial restriction-modification system, and annotated as a SAM hydrolase forming 5'-methyl-thioadenosine (MTA) and L-homoserine. From environmental phages, we recently discovered three SAMases with barely detectable sequence similarity to T3 SAMase and without homology to proteins of known structure. Here, we present the very first phage SAMase structures, in complex with a substrate analogue and the product MTA. The structure shows a trimer of alpha-beta sandwiches similar to the GlnB-like superfamily, with active sites formed at the trimer interfaces. Quantum-mechanical calculations, thin-layer chromatography, and nuclear magnetic resonance spectroscopy demonstrate that this family of enzymes are not hydrolases but lyases forming MTA and L-homoserine lactone in a unimolecular reaction mechanism. Sequence analysis and in vitro and in vivo mutagenesis support that T3 SAMase belongs to the same structural family and utilizes the same reaction mechanism.
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