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Each PKS module typically has three core catalytic domains: the β-ketoacyl-ACP synthase (KS), the acyltransferase (AT), and the acyl carrier protein (ACP). Most modules also carry specific combinations of ketoreductase (KR), dehydratase (DH), and enoylreductase (ER) tailoring domains.
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Each PKS module typically has three core catalytic domains: the β-ketoacyl-ACP synthase (KS), the acyltransferase (AT), and the acyl carrier protein (ACP). Most modules also carry specific combinations of ketoreductase (KR), dehydratase (DH), and enoylreductase (ER) tailoring domains.
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77958498759
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Although it is not essential to the application of the PPant ejection methodology, 2a-ACP and 3-ACP were cleanly resolved under the LC conditions used.
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Although it is not essential to the application of the PPant ejection methodology, 2a-ACP and 3-ACP were cleanly resolved under the LC conditions used.
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Dorrestein, P. C., Bumpus, S. B., Calderone, C. T., Garneau-Tsodikova, S., Aron, Z. D., Straight, P. D., Kolter, R., Walsh, C. T., and Kelleher, N. L. Biochemistry 2006, 45, 12756-12766
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58149494123
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The equilibrium for the FAS catalyzed dehydration to a disubstituted enoyl-ACP strongly also favors the hydrated form by ∼3:1. Cf.
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The equilibrium for the FAS catalyzed dehydration to a disubstituted enoyl-ACP strongly also favors the hydrated form by ∼3:1. Cf. Brown, A., Affleck, V., Kroon, J., and Slabas, A. FEBS Lett. 2009, 583, 363-368
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Castonguay, R., Valenzano, C. R., Chen, A. Y., Keatinge-Clay, A., Khosla, C., and Cane, D. E. J. Am. Chem. Soc. 2008, 130, 11598-11599
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Valenzano, C. R., Lawson, R. J., Chen, A. Y., Khosla, C., and Cane, D. E. J. Am. Chem. Soc. 2009, 131, 18501-18511
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77958449631
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The E -isomer 3 was cleanly resolved from the Z -isomer 5, and the two compounds were not interconverted under the conditions of the reaction.
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The E -isomer 3 was cleanly resolved from the Z -isomer 5, and the two compounds were not interconverted under the conditions of the reaction.
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21
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77958485402
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unpublished observations.
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You, Y.-O. and Cane, D. E., unpublished observations.
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Although DH4 processed both 2a-ACP and 6-ACP, DEBS DH4 does not dehydrate the corresponding SNAC thioester analog, anti -(2 R,3 R)- 2a-SNAC (ref 9). This observation is consistent with the presence of a presumptive ACP-binding region on the DH surface adjacent to the entrance to the substrate binding tunnel, a feature also found in bacterial FabZ proteins (ref 17).
-
Although DH4 processed both 2a-ACP and 6-ACP, DEBS DH4 does not dehydrate the corresponding SNAC thioester analog, anti -(2 R,3 R)- 2a-SNAC (ref 9). This observation is consistent with the presence of a presumptive ACP-binding region on the DH surface adjacent to the entrance to the substrate binding tunnel, a feature also found in bacterial FabZ proteins (ref 17).
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In the corresponding Type II FAS FabZ domains, a conserved Glu serves the same role as this Asp residue (ref 17).
-
In the corresponding Type II FAS FabZ domains, a conserved Glu serves the same role as this Asp residue (ref 17).
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