ArticleACS catalysis2023
Multiplexed Assessment of Promiscuous Non-Canonical Amino Acid Synthase Activity in a Pyridoxal Phosphate-Dependent Protein Family.
Article in ACS catalysis, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 16 citations in OpenAlex.
- A pyridoxal phosphate-dependent enzyme platform for stereoselective synthesis of γ-tertiary-nitro-noncanonical amino acids.Nature communications · 2026Article
- Flux sampling and context-specific genome-scale metabolic models for biotechnological applications.Trends in biotechnology · 2026Review
- Active site diversification of a non-canonical amino acid decarboxylase by merging substrate multiplexed screening with computationally guided recombination.Protein science : a publication of the Protein Society · 2025Article
- An efficient lysate-based approach for biosynthesis of the pyrrolobenzodiazepine natural product tilimycin.Journal of biotechnology · 2025Article
- α-Hydrazino Acids Inhibit Pyridoxal Phosphate-Dependent Decarboxylases via "Catalytically Correct" Ketoenamine Tautomers: A Special Motif for Chemical Biology and Drug Discovery?ACS catalysis · 2025Article
- Promiscuity Guided Evolution of Decarboxylative Aldolases for Synthesis of Tertiary γ-Hydroxy Amino Acids.Angewandte Chemie (International ed. in English) · 2025Article
- Chemoenzymatic Cascade Synthesis of Metal-ChelatingChemCatChem · 2025Article
- Substrate-Multiplexed Assessment of Aromatic Prenyltransferase Activity.Chembiochem : a European journal of chemical biology · 2025Article
- Molecular Basis for Cγ-N Bond Formation by PLP-Dependent Enzyme LolC.Biochemistry · 2024Article
- Elucidation of the stereochemical mechanism of cystathionine γ-lyase reveals how substrate specificity constrains catalysis.ACS catalysis · 2024Article
- Discovery and Characterization of Pyridoxal 5'-Phosphate-Dependent Cycloleucine Synthases.Journal of the American Chemical Society · 2024Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Pyridoxal phosphate (PLP)-dependent enzymes afford access to a variety of non-canonical amino acids (ncAAs), which are premier buildings blocks for the construction of complex bioactive molecules. The vinylglycine ketimine (VGK) subfamily of PLP-dependent enzymes plays a critical role in sulfur metabolism and is home to a growing set of secondary metabolic enzymes that synthesize γ-substituted ncAAs. Identification of VGK enzymes for biocatalysis faces a distinct challenge because the subfamily contains both desirable synthases as well as lyases that break down ncAAs. Some enzymes have both activities, which may contribute to pervasive mis-annotation. To navigate this complex functional landscape, we used a substrate multiplexed screening approach to rapidly measure the substrate promiscuity of 40 homologs in the VGK subfamily. We found that enzymes involved in transsulfuration are less likely to have promiscuous activities and often possess undesirable lyase activity. Enzymes from direct sulfuration and secondary metabolism generally had a high degree of substrate promiscuity. From this cohort, we identified an exemplary γ-synthase from
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