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. Author manuscript; available in PMC: 2010 Jun 2.
Published in final edited form as: Structure. 2006 Jan 26;14(3):611–621. doi: 10.1016/j.str.2006.01.001

Figure 6. Human Mutations Causing E3 Deficiency.

Figure 6

(A) The surface of the human E3 homodimer is shown as in Figure 3. One of the E3BD-binding sites is outlined in orange. Disease-causing mutations are colored dark blue (E340), red (D444), yellow (447), and magenta (R460). (B) Enzyme activities of wild-type and mutant human E3’s. The black bars represent E3 activity, the speckled bars show PDC activity reconstituted with wild-type and mutant E3. The identities of the E3’s used are shown on the x-axis. Activities are normalized to that of the wild-type enzymes, which at 100% are 314 s−1 for human E3 and 401 min−1 for the overall activity of the reconstituted PDC. (C) Dissociation constants (Kd) for the binding of wild-type and mutant E3 to LBD-E3BD as determined by ITC. NM, not measurable.