Fig. 3: Disproportionation of GNM P (7) and LNM E (8) to GNM B (4) and LNM E1 (2), and their corresponding hydrotrisulfides, revealing 4 and 2 as shunt metabolites in GNM and LNM biosynthesis. | Nature Communications

Fig. 3: Disproportionation of GNM P (7) and LNM E (8) to GNM B (4) and LNM E1 (2), and their corresponding hydrotrisulfides, revealing 4 and 2 as shunt metabolites in GNM and LNM biosynthesis.

From: Thiocysteine lyases as polyketide synthase domains installing hydropersulfide into natural products and a hydropersulfide methyltransferase

Fig. 3

a Disproportionation reaction of 7 or 8, generated in situ using 9 or 13 as a surrogate substrate, to 4 or 2 and the corresponding hydrotrisulfides, which can be trapped by GnmP in situ to afford the S-methylated trisulfide 12 or 15, respectively. b HPLC analysis of 7 disproportionation: (I) substrate 9, (II) 9 + WsmR-SH (boiled), (III) 9 + WsmR-SH, (IV) 9 + WsmR-SH + GnmP + SAM, (V) standard 4, and (VI) standard 3. Substrate and enzyme concentrations used: 9, 1 mM; SAM, 2 mM; WsmR-SH, 220 μM; and GnmP, 10 μM. Incubation time: 3 min for all assays. c HPLC analysis of 8 disproportionation: (I) substrate 13, (II) 13 + WsmR-SH (boiled), (III) 13 + WsmR-SH, (IV) 13 + WsmR-SH + GnmP + SAM, (V) standard 2, and (VI) standard 14. Substrate and enzyme concentrations used: 13, 5 mM, SAM, 10 mM; WsmR-SH, 220 μM; and GnmP, 10 μM. Incubation time: 3 min for assays II and III and 2 h for assay IV, respectively.

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