ArticleChembiochem : a European journal of chemical biology2025
Identification of a l-Threonine-Utilizing Hydrazine Synthetase for Thrazarine Biosynthesis in Streptomyces coerulescens MH802-fF5.
Article in Chembiochem : a European journal of chemical biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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1 citing paper in PubMed.
- tRNA-deacylase-directed discovery of biosynthetic pathways.Nature chemistry · 2026Article
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5 authors.
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Abstract
Hydrazine synthetases (HSs), consisting of cupin and methionyl-tRNA synthetase (MetRS)-like domains, catalyze hydrazine formation in the biosynthesis of various nitrogennitrogen (NN) bond-containing secondary metabolites. The structural diversity of the NN bond-containing secondary metabolites synthesized using this system is attributed to the diversity of amino acids (e.g., l-Glu, d-Glu, l-Ala, l-Tyr, l-Ser, and Gly) that are recognized by the MetRS domain. However, there are still many HS genes in the genome database whose substrates are unknown. This study identifies a putative biosynthetic gene cluster (BGC) for thrazarine, a diazo group-containing secondary metabolite with antitumor activity, by whole-genome sequencing of the thrazarine producer Streptomyces coerulescens MH802-fF5. In vivo and in vitro analyses showed that ThzN, an HS encoded by this BGC, synthesizes N-((5-carboxy-5-(amino)pentyl)amino)threonine from l-Thr and N
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