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Elucidation of the Cryptic Methyl Group Epimerase Activity of Dehydratase Domains From Modular Polyketide Synthases Using a Tandem Modules Epimerase Assay

Elucidation of the Cryptic Methyl Group Epimerase Activity of Dehydratase Domains From Modular Polyketide Synthases Using a Tandem Modules Epimerase Assay

Xinqiang Xie, Ashish Garg, Chaitan Khosla, David E Cane

J Am Chem Soc. 2017 Jul 19;139(28):9507-9510.

PMID: 28682630

Abstract:

Dehydratase (DH) domains of cryptic function are often found in polyketide synthase (PKS) modules that produce epimerized (2S)-2-methyl-3-ketoacyl-ACP (acyl carrier protein) intermediates. A combination of tandem equilibrium isotope exchange (EIX) and a newly developed Tandem Modules Epimerase assay revealed the intrinsic epimerase activity of NanDH1 and NanDH5, from modules 1 and 5, respectively, of the nanchangmycin (1) PKS as well of NigDH1, from module 1 of the nigericin (3) PKS. Unexpectedly, all three epimerase-active DH domains were also found to possess intrinsic dehydratase activity, whereas the conventional DH domains, EryDH4, from module 4 of the erythromycin synthase, and NanDH2 from module 2 of the nanchangmycin synthase, were shown to have cryptic epimerase activity.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP35865339	Nanchangmycin		35865-33-9	Price

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