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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.
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Enzyme Kinetics01:19

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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.
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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 Enzyme Kinetics01:19

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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.
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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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Binding sites linkages can regulate a protein's function.  For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
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Identification of Kinase-substrate Pairs Using High Throughput Screening
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Substrate selectivity APPLies to Akt.

Shimin Zhao1, Kun-Liang Guan

  • 1Laboratory of Molecular and Cellular Biology, Institute of Biomedical Sciences, Fudan University, Shanghai 200032, China.

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|May 6, 2008
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Summary
This summary is machine-generated.

The endosomal protein Appl1 regulates Akt signaling, influencing cell survival during zebrafish development. This discovery clarifies how Akt

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Area of Science:

  • Cellular signaling pathways
  • Molecular biology
  • Developmental biology

Background:

  • The protein kinase Akt is crucial in numerous signaling pathways.
  • While many Akt substrates are known, regulators of specific cellular responses to Akt signaling are less understood.

Discussion:

  • Schenck et al. (2008) identify the endosomal protein Appl1 as a key regulator of Akt signaling.
  • Appl1's role in modulating Akt's substrate selectivity is highlighted.

Key Insights:

  • Appl1 influences Akt's substrate selectivity, directing its signaling activity.
  • This modulation by Appl1 is essential for promoting cell survival in developing zebrafish.

Outlook:

  • Further research into Appl1 and its interactions could reveal new therapeutic targets.
  • Understanding Akt pathway regulation offers insights into developmental processes and disease.