SUMMARY
The authors describe an O-methyltransferase-like protein, AlpH, which is responsible for the hydrazine incorporation in kinamycin biosynthesis. To further test the aforementioned hypothesis in_vitro, Alp1W, AlpJ, and AlpK were expressed, and purified from Streptomyces or Escherichia coli and incubated with DHR, NADH, and gluN2H3 in a one-pot reaction (Supplementary Figs 3, 4). It possesses an N-terminal glycine rich motif, DFCGGQG, suggesting a putative SAM binding motif (DxGxGxG)27 (Supplementary Fig 6). To verify the function of AlpH in kinamycin biosynthesis, the authors generated an alpH in-frame deletion mutant strain, S. albus J1074 . . .
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