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Related Concept Videos

Ribozymes02:47

Ribozymes

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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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Enzymes02:34

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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.
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Introduction to Enzymes01:22

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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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Catalytically Perfect Enzymes01:07

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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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Cholinesterases: Distribution and Function01:22

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Cholinesterases are a group of serine hydrolase enzymes that play a crucial role in the breakdown of choline esters. The two primary types of cholinesterases are acetylcholinesterases (AChEs) and butyrylcholinesterase (BuChEs), which differ in their distribution, function, and substrate specificity. AChEs, also known as true cholinesterases, specifically hydrolyze acetylcholine, while BuChEs, often referred to as pseudocholinesterases, can hydrolyze various choline esters, including...
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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...
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Author Spotlight: Advancing Structural and Biochemical Studies of Proteins Through Thermal Shift Assays
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Emerging functions of pseudoenzymes.

Timea Goldberg1, Anju Sreelatha1,2

  • 1Department of Physiology, University of Texas Southwestern Medical Center, Dallas, TX, U.S.A.

The Biochemical Journal
|May 19, 2023
PubMed
Summary

Pseudoenzymes, proteins lacking typical catalytic motifs, are widespread and diverse. They perform crucial non-enzymatic functions and sometimes retain catalytic activity, warranting further study.

Keywords:
allosteric regulationcatalytic motifmolecular scaffoldsmolecular switchprotein moonlightingsubstrate trap

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Enzymology

Background:

  • Pseudoenzymes are increasingly recognized across diverse enzyme families and life forms.
  • Defined by the absence of conserved catalytic motifs, their evolutionary and functional roles are expanding.
  • These proteins can retain non-enzymatic functions like allosteric regulation, scaffolding, and signal integration.

Approach:

  • This review examines the prevalence and diversity of pseudoenzymes.
  • It analyzes methodologies for biochemical and functional characterization.
  • Examples from pseudokinase, pseudophosphatase, and pseudo ADP-ribosyltransferase families illustrate their functions.

Key Points:

  • Pseudoenzymes lack conserved catalytic motifs but may retain catalytic activity.
  • They serve vital non-enzymatic roles, including allosteric regulation and scaffolding.
  • Specific examples highlight the functional versatility of pseudoenzymes.

Conclusions:

  • Pseudoenzymes represent a significant and evolving area of biological research.
  • Understanding their diverse functions requires robust biochemical and functional characterization.
  • Further investigation into this burgeoning field is encouraged.