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. Author manuscript; available in PMC: 2014 Jan 24.
Published in final edited form as: Chem Biol. 2013 Jan 24;20(1):10.1016/j.chembiol.2012.10.020. doi: 10.1016/j.chembiol.2012.10.020

Figure 1. DhbE Catalyzed Aryl Acid Activation and the Yeast Selection Scheme to Change the Substrate Specificity of DhbE.

Figure 1

(A) DhbE catalyzes the condensation of DHB 1 with ATP to form DHB-AMP 2. The activated DHB is then transferred to the ArCP domain of DhbB to form a thioester conjugate 3 with the Ppant group of ArCP. DhbE can also activate SA 4. SA-AMS conjugate 5 is a bisubstrate inhibitor of DhbE. Structures of 3-HBA 6 and 2-ABA 7 as examples of nonnative substrates of DhbE are also shown.

(B) Selection of the A-domain library displayed on the surface of yeast cells. AMS-biotin conjugated SA (8) is used in the model selection to test the binding of wtDhbE on yeast cell surface with substrate-AMS conjugate. Compounds 9 and 10 have nonnative substrates 3-HBA 6 and 2-ABA 7 conjugated to AMS-biotin. They were used in the selection of DhbE mutants by yeast cell surface display.

See also Figures S1–S14 and Tables S1 and S3.