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

[Image: see text] 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-ketoacy...

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Autores principales: Ge, Hui-Ming, Huang, Tingting, Rudolf, Jeffrey D., Lohman, Jeremy R., Huang, Sheng-Xiong, Guo, Xun, Shen, Ben
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Chemical Society 2014
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4144755/
https://www.ncbi.nlm.nih.gov/pubmed/25019332
http://dx.doi.org/10.1021/ol501767v
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author Ge, Hui-Ming
Huang, Tingting
Rudolf, Jeffrey D.
Lohman, Jeremy R.
Huang, Sheng-Xiong
Guo, Xun
Shen, Ben
author_facet Ge, Hui-Ming
Huang, Tingting
Rudolf, Jeffrey D.
Lohman, Jeremy R.
Huang, Sheng-Xiong
Guo, Xun
Shen, Ben
author_sort Ge, Hui-Ming
collection PubMed
description [Image: see text] 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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spelling pubmed-41447552015-07-14 Enediyne Polyketide Synthases Stereoselectively Reduce the β-Ketoacyl Intermediates to β-d-Hydroxyacyl Intermediates in Enediyne Core Biosynthesis Ge, Hui-Ming Huang, Tingting Rudolf, Jeffrey D. Lohman, Jeremy R. Huang, Sheng-Xiong Guo, Xun Shen, Ben Org Lett [Image: see text] 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. American Chemical Society 2014-07-14 2014-08-01 /pmc/articles/PMC4144755/ /pubmed/25019332 http://dx.doi.org/10.1021/ol501767v Text en Copyright © 2014 American Chemical Society Terms of Use (http://pubs.acs.org/page/policy/authorchoice_termsofuse.html)
spellingShingle Ge, Hui-Ming
Huang, Tingting
Rudolf, Jeffrey D.
Lohman, Jeremy R.
Huang, Sheng-Xiong
Guo, Xun
Shen, Ben
Enediyne Polyketide Synthases Stereoselectively Reduce the β-Ketoacyl Intermediates to β-d-Hydroxyacyl Intermediates in Enediyne Core Biosynthesis
title Enediyne Polyketide Synthases Stereoselectively Reduce the β-Ketoacyl Intermediates to β-d-Hydroxyacyl Intermediates in Enediyne Core Biosynthesis
title_full Enediyne Polyketide Synthases Stereoselectively Reduce the β-Ketoacyl Intermediates to β-d-Hydroxyacyl Intermediates in Enediyne Core Biosynthesis
title_fullStr Enediyne Polyketide Synthases Stereoselectively Reduce the β-Ketoacyl Intermediates to β-d-Hydroxyacyl Intermediates in Enediyne Core Biosynthesis
title_full_unstemmed Enediyne Polyketide Synthases Stereoselectively Reduce the β-Ketoacyl Intermediates to β-d-Hydroxyacyl Intermediates in Enediyne Core Biosynthesis
title_short Enediyne Polyketide Synthases Stereoselectively Reduce the β-Ketoacyl Intermediates to β-d-Hydroxyacyl Intermediates in Enediyne Core Biosynthesis
title_sort enediyne polyketide synthases stereoselectively reduce the β-ketoacyl intermediates to β-d-hydroxyacyl intermediates in enediyne core biosynthesis
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4144755/
https://www.ncbi.nlm.nih.gov/pubmed/25019332
http://dx.doi.org/10.1021/ol501767v
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