Genome mining for mycemycin: discovery and elucidation of related methylation and chlorination biosynthetic chemistries
A silent dibenzoxazepinone (DBP) biosynthetic gene cluster (myc) was mutagenically
activated in Streptomyces olivaceus SCSIO T05, enabling the discovery of mycemycin C (4)
and three new analogues [mycemycins F–H (1–3)]. Gene disruption, complementation
experiments, and enzymatic assays unveiled salicylic acid and 5-Cl-kynurenine as
biosynthetic precursors and shed significant functional insights into MycO, MycB, MycR, and
MycJ, enzymes responsible for fine-tuning of the DBP scaffold.
activated in Streptomyces olivaceus SCSIO T05, enabling the discovery of mycemycin C (4)
and three new analogues [mycemycins F–H (1–3)]. Gene disruption, complementation
experiments, and enzymatic assays unveiled salicylic acid and 5-Cl-kynurenine as
biosynthetic precursors and shed significant functional insights into MycO, MycB, MycR, and
MycJ, enzymes responsible for fine-tuning of the DBP scaffold.
A silent dibenzoxazepinone (DBP) biosynthetic gene cluster (myc) was mutagenically activated in Streptomyces olivaceus SCSIO T05, enabling the discovery of mycemycin C (4) and three new analogues [mycemycins F–H (1–3)]. Gene disruption, complementation experiments, and enzymatic assays unveiled salicylic acid and 5-Cl-kynurenine as biosynthetic precursors and shed significant functional insights into MycO, MycB, MycR, and MycJ, enzymes responsible for fine-tuning of the DBP scaffold.
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