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Baeyer–Villiger oxidation converts aldehydes to carboxylic acids and ketones to esters. The reaction uses peroxy acids or peracids and is often catalyzed by acid. The reaction is named after its pioneers, Adolf von Baeyer and Victor Villiger. The reaction is achieved by a wide range of peracids such as m-chloroperoxybenzoic acid (mCPBA), perbenzoic acid (C6H5COOOH), peracetic acid (CH3COOOH), hydrogen peroxide (H2O2), and tert-butyl hydroperoxide (t-BuOOH).
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Intramolecular aldol reaction occurs in dicarbonyl compounds such as dialdehydes, diketones, and keto-aldehydes. The dicarbonyl compounds possess more than one nucleophilic ⍺ carbon for the base to deprotonate and form the enolates. For example, in symmetrical diketones, there are four ⍺ carbons. Hence, four types of enolates are possible when treated with a base. However, since the molecule is symmetrical, the enolates formed on either side of one carbonyl group are equivalent to those...
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Molecular Basis for Polyketide Ketoreductase-Substrate Interactions.

Shiji Zhao1,2, Fanglue Ni1, Tianyin Qiu1

  • 1Departments of Molecular Biology and Biochemistry, Chemical and Biomolecular Engineering, Materials Science and Engineering, and Biomedical Engineering, University of California, Irvine, CA 92697, USA.

International Journal of Molecular Sciences
|October 17, 2020
PubMed
Summary
This summary is machine-generated.

Researchers identified five key factors governing how ketoreductases (KRs) bind to substrates during polyketide biosynthesis. Understanding these molecular interactions aids in engineering polyketide synthases (PKSs) for novel compound discovery.

Keywords:
computational chemistryketoreductasemolecular dynamicsnatural productspolyketides

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Natural Product Synthesis

Background:

  • Polyketides are diverse natural products with significant bioactivities.
  • Type II polyketide synthases (PKSs) synthesize many polyketides using standalone enzymes.
  • Ketoreductases (KRs) are crucial for specific reduction steps, but their substrate interactions are poorly understood.

Purpose of the Study:

  • To computationally explore the molecular basis of ketoreductase (KR)-substrate interactions in type II polyketide synthases (PKSs).
  • To identify key factors that dictate substrate binding specificity and stability.
  • To provide insights for engineering PKSs and directing polyketide biosynthesis.

Main Methods:

  • Computational approaches were employed.
  • Analysis was based on previously solved apo and mimic cocrystal structures of KRs and their substrates.

Main Results:

  • Five key factors influencing KR-substrate binding were identified.
  • Two major substrate binding motifs were discovered.
  • Substrate length dictates binding position, and specific residues confer chain length specificity.
  • Substrate phosphorylation is critical for binding, and hydrophobic effects stabilize the complex.

Conclusions:

  • The study reveals the molecular determinants of KR-substrate interactions in type II PKSs.
  • These findings are valuable for the rational engineering of PKS enzymes.
  • The insights facilitate the directed biosynthesis of novel polyketides with desired bioactivities.