Enediyne Polyketide Synthases Stereoselectively Reduce the β-Ketoacyl Intermediates to β-d-Hydroxyacyl Intermediates in Enediyne Core Biosynthesis | Zendy

Hui Ming Ge | Zendy; Tingting Huang | Zendy; Jeffrey D. Rudolf | Zendy; Jeremy R. Lohman | Zendy; ShengXiong Huang | Zendy; Xun Guo | Zendy; Ben Shen | Zendy

Open Access

Enediyne Polyketide Synthases Stereoselectively Reduce the β-Ketoacyl Intermediates to β-d-Hydroxyacyl Intermediates in Enediyne Core Biosynthesis

Author(s) -

Hui Ming Ge,

Tingting Huang,

Jeffrey D. Rudolf,

Jeremy R. Lohman,

ShengXiong Huang,

Xun Guo,

Ben Shen

Publication year - 2014

Publication title -

organic letters

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.94

H-Index - 239

eISSN - 1523-7060

pISSN - 1523-7052

DOI - 10.1021/ol501767v

Subject(s) - enediyne , biosynthesis , polyketide , chemistry , stereochemistry , polyketide synthase , biochemistry , enzyme

PKSE biosynthesizes an enediyne core precursor from decarboxylative condensation of eight malonyl-CoAs. The KR domain of PKSE is responsible for iterative β-ketoreduction in each round of polyketide chain elongation. KRs from selected PKSEs were investigated in vitro with β-ketoacyl-SNACs as substrate mimics. Each of the KRs reduced the β-ketoacyl-SNACs stereoselectively, all affording the corresponding β-D-hydroxyacyl-SNACs, and the catalytic efficiencies (k(cat)/K(M)) of the KRs increased significantly as the chain length of the β-ketoacyl-SNAC substrate increases.

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