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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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Anaerobic Protein Purification and Kinetic Analysis via Oxygen Electrode for Studying DesB Dioxygenase Activity and Inhibition
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An efficient ribitol-specific dehydrogenase from Enterobacter aerogenes.

Ranjitha Singh1, Raushan Singh1, In-Won Kim1

  • 1Department of Chemical Engineering, Konkuk University, 1 Hwayang-Dong, Gwangjin-Gu, Seoul 143-701, South Korea.

Enzyme and Microbial Technology
|April 4, 2015
PubMed
Summary

Researchers cloned and expressed a novel NAD(+)-dependent ribitol dehydrogenase (EaRDH) from Enterobacter aerogenes. This enzyme displays unique substrate specificity and high activity, offering potential applications in biotechnology.

Keywords:
Enterobacter aerogenesHomology modelingRibitol dehydrogenaseShort-chain dehydrogenase/reductase

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Area of Science:

  • Biochemistry
  • Enzymology
  • Molecular Biology

Background:

  • NAD(+)-dependent ribitol dehydrogenases (RDHs) are crucial enzymes in polyol metabolism.
  • Understanding the structure-function relationship of RDHs can reveal novel catalytic mechanisms and applications.

Purpose of the Study:

  • To clone, express, and characterize a novel NAD(+)-dependent ribitol dehydrogenase (EaRDH) from Enterobacter aerogenes.
  • To investigate the biochemical properties, substrate specificity, and structural basis of EaRDH activity.

Main Methods:

  • Gene cloning and expression in Escherichia coli.
  • Enzyme purification using nickel affinity chromatography.
  • Biochemical assays to determine optimal conditions and kinetic parameters.
  • Homology modeling and docking analysis for structural insights.

Main Results:

  • EaRDH was successfully cloned, expressed, and purified as an active soluble enzyme.
  • The enzyme exhibited optimal activity at pH 11.0 and 45°C, with high specificity for ribitol and NAD(+).
  • Kinetic analysis revealed high catalytic efficiency (kcat/Km = 30.9s⁻¹mM⁻¹).
  • Structural analysis provided insights into its unique substrate specificity and high activity.

Conclusions:

  • EaRDH is a novel, highly active, and specific NAD(+)-dependent ribitol dehydrogenase.
  • Its unique biochemical and structural properties distinguish it from other known RDHs.
  • EaRDH holds potential for biotechnological applications requiring specific ribitol oxidation.