ArticleChembiochem : a European journal of chemical biology2022
Investigation of β-Substitution Activity of O-Acetylserine Sulfhydrolase from Citrullus vulgaris.
Article in Chembiochem : a European journal of chemical biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 6 citations in OpenAlex.
- A pyridoxal phosphate-dependent enzyme platform for stereoselective synthesis of γ-tertiary-nitro-noncanonical amino acids.Nature communications · 2026Article
- Benzoic and salicylic acids inhibit β-substituted alanine synthase 4;1 in common bean.Plant physiology · 2025Article
- An Update: Enzymatic Synthesis for Industrial Applications.Angewandte Chemie (International ed. in English) · 2025Review
- Multiplexed Assessment of Promiscuous Non-Canonical Amino Acid Synthase Activity in a Pyridoxal Phosphate-Dependent Protein Family.ACS catalysis · 2023Article
- Investigation of β-Substitution Activity of O-Acetylserine Sulfhydrolase from Citrullus vulgaris.Chembiochem : a European journal of chemical biology · 2022Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Pyridoxal-5'-phosphate (PLP)-dependent enzymes have garnered interest for their ability to synthesize non-standard amino acids (nsAAs). One such class of enzymes, O-acetylserine sulfhydrylases (OASSs), catalyzes the final step in the biosynthesis of l-cysteine. Here, we examine the β-substitution capability of the OASS from Citrullus vulgaris (CvOASS), a putative l-mimosine synthase. While the previously reported mimosine synthase activity was not reproducible in our hands, we successfully identified non-native reactivity with a variety of O-nucleophiles. Optimization of reaction conditions for carboxylate and phenolate substrates led to distinct conditions that were leveraged for the preparative-scale synthesis of nsAAs. We further show this enzyme is capable of C-C bond formation through a β-alkylation reaction with an activated nitroalkane. To facilitate understanding of this enzyme, we determined the crystal structure of the enzyme bound to PLP as the internal aldimine at 1.55 Å, revealing key features of the active site and providing information that may guide subsequent development of CvOASS as a practical biocatalyst.
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