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Related Concept Videos

Introduction to Enzyme Kinetics01:19

Introduction to Enzyme Kinetics

Enzyme kinetics studies the rates of biochemical reactions. Scientists monitor the reaction rates for a particular enzymatic reaction at various substrate concentrations. Additional trials with inhibitors or other molecules that affect the reaction rate may also be performed.
The experimenter can then plot the initial reaction rate or velocity (Vo) of a given trial against the substrate concentration ([S]) to obtain a graph of the reaction properties. For many enzymatic reactions involving a...
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.
Evolution of New Traits in Microbes01:24

Evolution of New Traits in Microbes

Microorganisms evolve rapidly due to their large population sizes and short generation times, often exhibiting measurable changes within days under laboratory conditions. Natural selection acts on standing genetic variation, enabling the retention and amplification of beneficial traits that confer fitness advantages in changing environments.Adaptive Pigment Regulation in RhodobacterIn Rhodobacter, a genus of purple non-sulfur bacteria, light-harvesting pigments such as bacteriochlorophyll and...
Enzyme Kinetics01:19

Enzyme Kinetics

Enzymes speed up reactions by lowering the activation energy of the reactants. The speed at which the enzyme turns reactants into products is called the rate of reaction. Several factors impact the rate of reaction, including the number of available reactants. Enzyme kinetics is the study of how an enzyme changes the rate of a reaction.
Scientists typically study enzyme kinetics with a fixed amount of enzyme in the controlled environment of a test tube. When more reactant, or substrate, is...
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...

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A New Screening Method for the Directed Evolution of Thermostable Bacteriolytic Enzymes
13:30

A New Screening Method for the Directed Evolution of Thermostable Bacteriolytic Enzymes

Published on: November 7, 2012

Toward a systems biology perspective on enzyme evolution.

Shelley D Copley1

  • 1Department of Molecular, Cellular and Developmental Biology and Cooperative Institute for Research in Environmental Sciences, University of Colorado at Boulder, Boulder, Colorado 80309.

The Journal of Biological Chemistry
|November 10, 2011
PubMed
Summary

Enzyme evolution occurs through gene duplication and divergence, leading to specialized functions and novel enzyme development. Microbial enzyme evolution depends on existing networks, environment, and functional trade-offs.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Evolutionary Biology

Background:

  • Enzymes evolve from common ancestors via gene duplication and divergence.
  • Early enzymes were generalists; specialization enhanced catalysis and metabolic control.

Purpose of the Study:

  • To explore the evolutionary pathways of enzyme superfamilies.
  • To understand the emergence of novel enzymatic functions.

Main Methods:

  • Analysis of gene duplication and divergence events.
  • Examination of metabolic networks and enzyme function evolution.

Main Results:

  • Specialized enzymes evolved from generalist ancestors, improving catalytic efficiency.
  • Novel enzymes arose from secondary activities within specialized enzymes.
  • Enzyme evolution is influenced by gene collections, network topology, and environmental factors.

Conclusions:

  • Enzyme evolution is a complex process driven by gene duplication, divergence, and functional specialization.
  • The evolution of new enzymes is constrained by existing metabolic networks and environmental pressures, involving trade-offs between original and novel activities.