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Related Concept Videos

Introduction to Mechanisms of Enzyme Catalysis01:13

Introduction to Mechanisms of Enzyme Catalysis

For many years, scientists thought that enzyme-substrate binding took place in a simple "lock-and-key" fashion. This model stated that the enzyme and substrate fit together perfectly in one instantaneous step. However, current research supports a more refined view scientists call induced fit. The induced-fit model expands upon the lock-and-key model by describing a more dynamic interaction between enzyme and substrate. As the enzyme and substrate come together, their interaction causes a mild...
Introduction to Mechanisms of Enzyme Catalysis01:13

Introduction to Mechanisms of Enzyme Catalysis

For many years, scientists thought that enzyme-substrate binding took place in a simple "lock-and-key" fashion. This model stated that the enzyme and substrate fit together perfectly in one instantaneous step. However, current research supports a more refined view scientists call induced fit. The induced-fit model expands upon the lock-and-key model by describing a more dynamic interaction between enzyme and substrate. As the enzyme and substrate come together, their interaction causes a mild...
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...
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.
Introduction to Enzymes01:22

Introduction to Enzymes

The use of enzymes by humans dates to 7000 BCE. Humans first used enzymes to ferment sugars and produce alcohol without knowing that this was an enzyme-catalyzed reaction. Wilhelm Kuhne coined the term 'enzyme' in 1877 from the Greek words ‘en’ meaning ‘in’ or ‘within’ and ‘zyme’ meaning ‘yeast.’
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Introduction To Enzymes01:22

Introduction To Enzymes

The use of enzymes by humans dates to 7000 BCE. Humans first used enzymes to ferment sugars and produce alcohol without knowing that this was an enzyme-catalyzed reaction. Wilhelm Kuhne coined the term 'enzyme' in 1877 from the Greek words ‘en’ meaning ‘in’ or ‘within’ and ‘zyme’ meaning ‘yeast.’
Most enzymes are proteins that speed up biochemical reactions without being consumed. Enzymes contain one or more active sites that bind the substrates and convert them into products. Many enzymes also...

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Measuring Enzymatic Stability by Isothermal Titration Calorimetry
08:37

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Published on: March 26, 2019

Structural stability of an enzyme biocatalyst.

P A Dalby1, J P Aucamp, R George

  • 1The Advanced Centre for Biochemical Engineering, Department of Biochemical Engineering, UCL (University College London), Torrington Place, London WC1E 7JE, U.K. p.dalby@ucl.ac.uk

Biochemical Society Transactions
|November 23, 2007
PubMed
Summary

Transketolase (TK) inactivation in biocatalysis involves complex denaturation pathways. Understanding these mechanisms, including cofactor interactions and intermediate states, is key to improving enzyme stability and process efficiency.

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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
  • Enzyme Kinetics
  • Protein Chemistry

Background:

  • Transketolase (TK) is prone to inactivation during biocatalysis through various mechanisms like oxidation, inhibition, and cofactor dissociation.
  • The precise role of protein denaturation in these inactivation pathways remains incompletely understood.

Purpose of the Study:

  • To characterize the urea-induced reversible denaturation of Escherichia coli TK apo- and holo-enzyme forms.
  • To investigate the reconstitution pathway of holo-TK from apoenzyme and cofactors.
  • To explore the impact of oxidizing conditions on TK deactivation mechanisms.

Main Methods:

  • Urea-induced denaturation studies on E. coli TK apo- and holo-enzymes.
  • Enzyme reconstitution assays.
  • Analysis of intermediate states during denaturation and reconstitution.
  • Preliminary studies under oxidizing conditions.

Main Results:

  • Identified an unusual intermediate state where cofactors are bound but the enzyme is inactive, occurring in both reconstitution and denaturation pathways.
  • Demonstrated convergence of holo- and apoenzyme denaturation pathways at a partially denatured apo-homodimer intermediate.
  • Preliminary findings suggest increased complexity in deactivation mechanisms under oxidizing conditions.

Conclusions:

  • Protein denaturation significantly contributes to TK inactivation, involving distinct intermediate states.
  • The study elucidates complex denaturation and reconstitution pathways for TK, highlighting cofactor-bound inactive intermediates.
  • Further research into oxidative stress is needed to fully understand biocatalytic enzyme deactivation.