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Related Concept Videos

Allosteric Proteins-ATCase01:19

Allosteric Proteins-ATCase

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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ATP synthase or ATPase is among the most conserved proteins found in bacteria, mammals, and plants. This enzyme can catalyze a forward reaction in response to the electrochemical gradient, producing ATP from ADP and inorganic phosphate. ATP synthase can also work in a reverse direction by hydrolyzing ATP and generating an electrochemical gradient. Different forms of ATP synthases have evolved special features to meet the specific demands of the cell. Based on their specific feature, ATP...
Enzyme-linked Receptors01:00

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Enzymes02:34

Enzymes

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Related Experiment Video

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Determining the Serum Stability of Human Adenosine Deaminase 1 Enzyme
04:17

Determining the Serum Stability of Human Adenosine Deaminase 1 Enzyme

Published on: September 27, 2024

Adenylate-forming enzymes.

Stefan Schmelz1, James H Naismith

  • 1Scottish Structural Proteomics Facility and Biomedical Science Research Complex, The University of St Andrews, Scotland KY16 9ST, UK.

Current Opinion in Structural Biology
|October 20, 2009
PubMed
Summary
This summary is machine-generated.

This review proposes a new classification for adenylate enzymes, which activate carboxylic acids using adenosine monophosphate. These enzymes are crucial for forming bonds in natural products.

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Determining the Serum Stability of Human Adenosine Deaminase 1 Enzyme
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Using Modified Synthetic Oligonucleotides to Assay Nucleic Acid-Metabolizing Enzymes

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Area of Science:

  • Biochemistry
  • Enzymology
  • Organic Chemistry

Background:

  • Thioesters, amides, and esters are fundamental linkages in natural products.
  • Enzyme catalysis offers efficient routes for synthesizing these chemical bonds.
  • Adenylate enzymes activate carboxylic acids via adenosine monophosphate (AMP) formation, a key strategy in biosynthesis.

Purpose of the Study:

  • To propose a novel classification scheme for adenylate enzymes.
  • To review recent advancements in the study of adenylate enzymes.
  • To highlight the evolutionary diversity of these enzymes.

Main Methods:

  • Literature review of adenylate enzyme studies.
  • Analysis of enzyme structure, active site, and metal coordination.
  • Development of a new enzyme classification system.

Main Results:

  • Adenylate enzymes exhibit significant diversity in their three-dimensional folds.
  • Active site architectures vary considerably among different adenylate enzymes.
  • Diverse metal coordination strategies are employed by these enzymes.

Conclusions:

  • A new classification system for adenylate enzymes is presented.
  • The evolutionary adaptations in enzyme fold, active site, and metal binding are highlighted.
  • Understanding this diversity aids in the study of natural product biosynthesis.