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. Author manuscript; available in PMC: 2016 Oct 27.
Published in final edited form as: Biochemistry. 2015 Oct 9;54(42):6462–6474. doi: 10.1021/acs.biochem.5b00532

Figure 7.

Figure 7

The Fe–S cluster of Asp inhibits its phosphatase activity and unmasks its kinase activity. Panel A shows the phosphatase activity of Asp1371–920 (0.5 μg/mL) against 10 μM 1,5-InsP8 as substrate, following “reconstitution” of the protein in buffer with or without Fe3+,2+ and/or S2− as indicated. Panel B shows similar experiments except the added protein was either full length wild-type (“WT”) or the Asp1H807A mutant (0.7 μg/mL).