Fig. 1
From: GyrI-like proteins catalyze cyclopropanoid hydrolysis to confer cellular protection
Structures of cyclopropapyrroloindole compounds and characterization of cyclopropanoid cyclopropyl hydrolases (CCHs). a Structures of yatakemycin (YTM), CC-1065, and duocarmycins. 1 L, 1 M, and 1 R indicate the three subunits of YTM, respectively. The IC50 reveals the cytotoxicity against L1210 cell line. b Genetic investigation of ytkR7 by HPLC analysis of the fermentation products (UV at 383 nm). (i) wild-type Streptomyces sp. TP-A0356; (ii) the ΔytkR7 mutant Streptomyces sp. TG1310; (iii) the ΔytkR7 mutant complemented with the ytkR7 gene in trans; and (iv) the ΔytkR7 mutant complemented with the c10R6 gene from S. zelensis NRRL 11183. c Structures of compounds 5, 6, and 7. d Biochemical characterization of YtkR7 with YTM as substrate. (i) YTM dissolved in the reaction buffer; (ii) boiled YtkR7; (iii) YtkR7; and (iv) standard of 5. e Biochemical assays of the other selected CCHs using YTM as substrate. (i) C10R6; (ii) lin2189 from Listeria innocua Clip11262; (iii) ETI84332.1 from Streptococcus anginosus DORA_7 (from the human microbiota); and (iv) MA1133 from Methanosarcina acetivorans C2A. f Characterization of substrate specificity of the CCH protein C10R6 by HPLC analysis (UV at 374 nm). (i) CC-1065 dissolved in the reaction buffer; (ii) C10R6 with CC-1065 as substrate; (iii) the fermentation products of S. zelensis NRRL 11183; and (iv) standard of 7
