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Related Concept Videos

Catalytically Perfect Enzymes01:07

Catalytically Perfect Enzymes

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The theory of catalytically perfect enzymes was first proposed by W.J. Albery and J. R. Knowles in 1976. These enzymes catalyze biochemical reactions at high-speed. Their catalytic efficiency values range from 108-109 M-1s-1. These enzymes are also called 'diffusion-controlled' as the only rate-limiting step in the catalysis is that of the substrate diffusion into the active site. Examples include triose phosphate isomerase, fumarase, and superoxide dismutase.
 
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Chemical reactions often occur in a stepwise fashion involving two or more distinct reactions taking place in a sequence. A balanced equation indicates the reacting species and the product species, but it reveals no details about how the reaction occurs at the molecular level. The reaction mechanism (or reaction path) provides details regarding the precise, step-by-step process by which a reaction occurs. Each of the steps in a reaction mechanism is called an elementary reaction. These...
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Inhibitors are molecules that reduce enzyme activity by binding to the enzyme. In a normally functioning cell, enzymes are regulated by a variety of inhibitors. Drugs and other toxins can also inhibit enzymes. Some inhibitors bind to the enzyme’s active site, while others inhibit enzymatic activity by binding to other sites on the protein structure.
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Phase II reactions are essential for the detoxification and elimination of drugs from the body. These reactions involve the conjugation of parent drugs or their phase I metabolites with endogenous molecules, resulting in more hydrophilic drug conjugates. The primary conjugation reactions in this phase are sulfation and glucuronidation. Both sulfation and glucuronidation typically produce biologically inactive metabolites. However, in some cases involving prodrugs, active metabolites may be...
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Updated: Dec 23, 2025

Biosynthesis of a Flavonol from a Flavanone by Establishing a One-pot Bienzymatic Cascade
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Phase-Separated Multienzyme Biosynthesis.

Miao Liu1, Sicong He2, Lixin Cheng3

  • 1Department of Chemistry, School of Life Sciences, The Chinese University of Hong Kong, Shatin, Hong Kong SAR, China.

Biomacromolecules
|April 29, 2020
PubMed
Summary
This summary is machine-generated.

Liquid-liquid phase separation creates protein condensates that enhance multienzyme biocatalysis. This study demonstrates synthetic condensates accelerate key biosynthetic pathways, boosting production rates.

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Area of Science:

  • Biochemistry and Molecular Biology
  • Biophysics
  • Synthetic Biology

Background:

  • Liquid-liquid phase separation (LLPS) drives the formation of dynamic cellular condensates, such as the purinosome, essential for metabolic processes.
  • Multienzyme complexes within condensates facilitate efficient biochemical reactions through proximity and substrate channeling.

Purpose of the Study:

  • To engineer synthetic multienzyme systems using protein phase separation to enhance biocatalytic efficiency.
  • To investigate the impact of condensate formation on the activity of enzymes in specific biosynthetic pathways.

Main Methods:

  • Utilized a synthetic protein phase separation system based on GKAP, Shank, and Homer proteins.
  • Assembled guest proteins, including fluorescent proteins (CFP, YFP) and enzymes from menaquinone (MenF, MenD, MenH) and terpene (Idi, IspA) biosynthesis pathways, within the condensates via peptide-peptide interactions.
  • Measured Förster Resonance Energy Transfer (FRET) signal distribution and quantified production rates of key metabolites.

Main Results:

  • Observed a broad distribution of FRET signals upon coassembly of CFP and YFP, indicating dynamic interactions within the condensate.
  • Demonstrated a 70% increase in 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate production by spontaneous enrichment of the rate-limiting enzyme MenD.
  • Achieved over 50% increase in farnesyl pyrophosphate production by coassembling Idi and IspA enzymes within the protein condensate.

Conclusions:

  • Protein phase separation provides a robust platform for constructing functional synthetic multienzyme systems.
  • Engineered condensates significantly accelerate multienzyme biocatalysis, offering a promising strategy for metabolic engineering and synthetic biology applications.