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Related Concept Videos

Catalytically Perfect Enzymes01:07

Catalytically Perfect Enzymes

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.
Lysosomal Hydrolases01:22

Lysosomal Hydrolases

Lysosomes are the site for the degradation of macromolecules and biological polymers released during membrane trafficking events such as secretory, endocytic, autophagic, and phagocytic pathways. The membrane-enclosed area of the lysosome, called the lumen, contains hydrolytic enzymes active in an acidic environment. These acid hydrolases are functional at a pH between 4.5 and 5 and are involved in cellular processes such as cell signaling, energy metabolism, restoration of the plasma membrane,...
Induced-fit Model01:13

Induced-fit Model

Most chemical reactions in cells require enzymes—biological catalysts that speed up the reaction without being consumed or permanently changed. They reduce the activation energy needed to convert the reactants into products. Enzymes are proteins, that usually work by binding to a substrate—a reactant molecule that they act upon.
Enzymes exhibit substrate specificity, meaning that they can only bind to certain substrates. This is mainly determined by the shape and chemical characteristics of...
Enzymes02:34

Enzymes

Inside living organisms, enzymes act as catalysts for many biochemical reactions involved in cellular metabolism. The role of enzymes is to reduce the activation energies of biochemical reactions by forming complexes with its substrates. The lowering of activation energies favor an increase in the rates of biochemical reactions.
Enzyme deficiencies can often translate into life-threatening diseases. For example, a genetic abnormality resulting in the deficiency of the enzyme G6PD...
ATP Synthase: Structure01:18

ATP Synthase: Structure

ATP synthase or ATPase is among the most conserved proteins found in bacteria, mammals, and plants. This enzyme can catalyze a forward reaction in response to the electrochemical gradient, producing ATP from ADP and inorganic phosphate. ATP synthase can also work in a reverse direction by hydrolyzing ATP and generating an electrochemical gradient. Different forms of ATP synthases have evolved special features to meet the specific demands of the cell. Based on their specific feature, ATP...
Hydrolysis01:15

Hydrolysis

Overview
Hydrolysis is a chemical reaction in which the addition of water breaks down a polymer into its simpler monomer units. For example, peptides break into amino acids, carbohydrates into simple sugars, and DNA into nucleotides. Enzymes often facilitate these processes.
Hydrolysis Reverses Dehydration Synthesis
Complex carbohydrates can be broken down by breaking the bonds between individual sugar units. The reaction breaks a glycosidic bond as water is added to the compound. The...

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Related Experiment Video

Updated: May 29, 2026

Synthesis of an Intein-mediated Artificial Protein Hydrogel
15:06

Synthesis of an Intein-mediated Artificial Protein Hydrogel

Published on: January 27, 2014

A Highly Efficient Artificial Hydrolase with a Well-Defined Dynamic Active Center.

Yan Wang1, Yi Cao1, Yuan-Yuan Liu1

  • 1Institute of Nanochemistry and Nanobiology, Shanghai University, Shanghai 200444, China.

ACS Applied Materials & Interfaces
|May 27, 2026
PubMed
Summary

Researchers developed Goldenzyme, an artificial hydrolase using conformational engineering on gold nanoparticles. This enzyme mimic exhibits fast dynamics and synergistic active sites, outperforming natural enzymes in certain reactions and addressing environmental challenges.

Keywords:
artificial enzymecatalytic triadconformational engineeringdynamic conformationnanoparticle

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Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes
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Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes

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Last Updated: May 29, 2026

Synthesis of an Intein-mediated Artificial Protein Hydrogel
15:06

Synthesis of an Intein-mediated Artificial Protein Hydrogel

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Expression, Purification, Crystallization, and Enzyme Assays of Fumarylacetoacetate Hydrolase Domain-Containing Proteins
10:21

Expression, Purification, Crystallization, and Enzyme Assays of Fumarylacetoacetate Hydrolase Domain-Containing Proteins

Published on: June 20, 2019

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes
09:42

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes

Published on: January 16, 2016

Area of Science:

  • Biochemistry
  • Nanotechnology
  • Enzyme Engineering

Background:

  • Current artificial hydrolases lack essential features of natural enzymes, such as fast active site dynamics and synergistic catalytic components.
  • Achieving high catalytic turnover numbers (kcat) in artificial enzymes remains a significant challenge.

Purpose of the Study:

  • To engineer a gold nanoparticle (AuNP)-based artificial hydrolase, Goldenzyme, mimicking the catalytic triad, oxyanion hole, and binding site of alpha-chymotrypsin (α-CT).
  • To incorporate fast-dynamics and synergistic active site features into artificial enzymes.

Main Methods:

  • Conformational engineering (CE) approach to reconstruct key α-CT active site components on AuNPs.
  • Nuclear Magnetic Resonance (NMR) experiments to assess the dynamic properties of Goldenzyme.
  • Mutation experiments to validate the roles of key residues and their synergy.

Main Results:

  • Goldenzyme demonstrated fast-dynamics, approximately 5-fold faster than a typical alpha-helix.
  • Mutation studies confirmed the essential roles and synergy of the catalytic triad, oxyanion hole, and binding site.
  • Goldenzyme achieved a kcat of 6.4 s⁻¹ for p-nitrophenyl acetate hydrolysis, exceeding α-CT's kcat (1.2 s⁻¹).
  • Goldenzyme successfully hydrolyzed phthalate esters (PAEs), which α-CT could not.

Conclusions:

  • Conformational engineering is a viable strategy for creating artificial enzymes with enhanced catalytic activity and functional features.
  • Goldenzyme represents a significant advancement in artificial enzyme design, showcasing the importance of dynamics and active site synergy.
  • The CE approach shows promise for application to other nanomaterials, such as silica NPs, for broader applications.