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Related Concept Videos

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...
Ribozymes02:47

Ribozymes

The term ribozyme is used for RNA that can act as an enzyme. Ribozymes are mainly found in selected viruses, bacteria, plant organelles, and lower eukaryotes. Ribozymes were first discovered in 1982 when Tom Cech’s laboratory observed Group I introns acting as enzymes. This was shortly followed by the discovery of another ribozyme, Ribonulcease P, by Sid Altman’s laboratory. Both Cech and Altman received the Nobel Prize in chemistry in 1989 for their work on ribozymes.
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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...
Ribozymes02:47

Ribozymes

The term ribozyme is used for RNA that can act as an enzyme. Ribozymes are mainly found in selected viruses, bacteria, plant organelles, and lower eukaryotes. Ribozymes were first discovered in 1982 when Tom Cech’s laboratory observed Group I introns acting as enzymes. This was shortly followed by the discovery of another ribozyme, Ribonulcease P, by Sid Altman’s laboratory. Both Cech and Altman received the Nobel Prize in chemistry in 1989 for their work on ribozymes.
Ribozymes can be...
Introduction to Mechanisms of Enzyme Catalysis01:13

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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...

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Nanomanipulation of Single RNA Molecules by Optical Tweezers
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Published on: August 20, 2014

Capturing hammerhead ribozyme structures in action by modulating general base catalysis.

Young-In Chi1, Monika Martick, Monica Lares

  • 1Department of Molecular and Cellular Biochemistry, Center for Structural Biology, University of Kentucky, Lexington, Kentucky, United States of America. ychi@uky.edu

Plos Biology
|October 7, 2008
PubMed
Summary
This summary is machine-generated.

Crystal structures reveal hammerhead ribozyme mechanisms. Researchers obtained precatalytic and postcatalytic structures of a self-cleaving RNA enzyme, uncovering key interactions for catalytic activity.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • RNA Catalysis

Background:

  • Hammerhead ribozymes are crucial RNA enzymes catalyzing self-cleavage.
  • Understanding their catalytic mechanism requires high-resolution structural data of reaction intermediates.

Purpose of the Study:

  • To elucidate the structural basis of hammerhead ribozyme catalysis.
  • To capture and characterize enzyme-substrate and enzyme-product complexes of a self-cleaving hammerhead ribozyme.

Main Methods:

  • Obtained precatalytic and postcatalytic crystal structures of a full-length hammerhead ribozyme.
  • Utilized the satellite tobacco ringspot virus hammerhead RNA sequence.
  • Modified the general base (G12 to A12) to slow cleavage and enable complex isolation.

Main Results:

  • Captured crystal structures of both enzyme-substrate and enzyme-product complexes.
  • The enzyme-product complex structure reveals RNA and metal ion interactions potentially involved in transition-state stabilization.
  • These interactions are absent in the precatalytic structures, providing insights into the reaction pathway.

Conclusions:

  • The study provides unprecedented structural snapshots of hammerhead ribozyme catalysis.
  • Identified specific RNA-metal ion interactions crucial for stabilizing the transition state.
  • Offers a deeper mechanistic understanding of RNA-mediated cleavage reactions.