A Bifunctional Methyltransferase in Biosynthesis of Antitumor Antibiotic Streptonigrin

• Published in: Chembiochem : a European journal of chemical biology Vol. 25; no. 18; pp. e202400292 - n/a
• Main Authors: Wang, Xiaozheng, Xie, Xinyue, Wo, Jing, Huang, Tingting, Deng, Zixin, Lin, Shuangjun
• Format: Journal Article
• Language: English
• Published: Germany Wiley Subscription Services, Inc 16.09.2024
• Subjects: Antibiotics; Antibiotics, Antineoplastic - biosynthesis; Antibiotics, Antineoplastic - chemistry; Antibiotics, Antineoplastic - metabolism; Antibiotics, Antineoplastic - pharmacology; Anticancer properties; Antitumor activity; Biosynthesis; Carboxyl group; Hydroxyl groups; Methylation; Methyltransferase; Methyltransferases - metabolism; StnQ2; Streptomyces - enzymology; Streptomyces - metabolism; Streptonigrin; Streptonigrin - chemistry; Streptonigrin - metabolism; Biosynthesis; StnQ2; Methyltransferase; Streptonigrin
• ISSN: 1439-4227; 1439-7633; 1439-7633
• DOI: 10.1002/cbic.202400292

Streptonigrin (STN, 1) is a highly functionalized aminoquinone alkaloid antibiotic with broad and potent antitumor activity. STN structurally contains four methyl groups belonging to two types: C‐methyl group and O‐methyl groups. Here, we report the biochemical characterization of the O‐methyltransferase StnQ2 that can catalyze both the methylation of a hydroxyl group and a carboxyl group in the biosynthesis of streptonigrin. This work not only provides a new insight into methyltransferases, but also advances the elucidation of the complete biosynthetic pathway of streptonigrin. StnQ2 was biochemically characterized to be a bifunctional methyltransferase that can catalyze both the methylation of a hydroxyl group and a carboxyl group. This work deepens our understanding of the methyltransferase, laying the groundwork for the elucidation of the complete biosynthesis pathway of streptonigrin.