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Related Concept Videos

Cholera01:25

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Cholera is an acute gastrointestinal disease caused by the Gram-negative bacterium Vibrio cholerae. It is transmitted primarily via the fecal-oral route through the ingestion of contaminated water or food.Vibrio cholerae is a motile, Gram-negative bacterium of the family Vibrionaceae, primarily associated with waterborne outbreaks in areas with inadequate sanitation. Although over 200 serogroups of V. cholerae exist, only O1 and O139 are responsible for epidemic cholera. The O1 serogroup,...
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Differential staining is an essential microbiological technique that exploits variations in cell wall structures to classify and identify microorganisms. It facilitates the distinction of bacteria, aiding in diagnostic and research applications. Two of the most widely used differential staining methods are Gram staining and acid-fast staining, both of which rely on the chemical and structural differences in bacterial cell walls.Gram Staining TechniqueGram staining differentiates bacteria by...
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Two basic types of preparation are used to visualize specimens with a light microscope: wet mounts and fixed specimens.
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A Dye-Decolorizing Peroxidase from Vibrio cholerae.

Takeshi Uchida1,2, Miho Sasaki2, Yoshikazu Tanaka3

  • 1Department of Chemistry, Faculty of Science, Hokkaido University , Sapporo 060-0810, Japan.

Biochemistry
|October 3, 2015
PubMed
Summary

Vibrio cholerae dye-decolorizing peroxidase (VcDyP) shows pH-dependent activity, utilizing specific tyrosine residues for dye degradation at low pH and forming covalent bonds at higher pH. This suggests a pH-switchable radical transfer pathway for survival in harsh conditions.

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Area of Science:

  • Biochemistry
  • Enzymology
  • Protein Science

Background:

  • Dye-decolorizing peroxidases (DyPs) are enzymes capable of degrading various dyes.
  • The specific functions and mechanisms of DyPs from different bacterial species are not fully understood.

Purpose of the Study:

  • To characterize the dye-decolorizing peroxidase (DyP) from Vibrio cholerae (VcDyP).
  • To elucidate the kinetic properties, active site residues, and pH-dependent mechanism of VcDyP.
  • To investigate the role of VcDyP in bacterial survival under stress conditions.

Main Methods:

  • Expression and purification of VcDyP in E. coli.
  • Assay of DyP activity using Reactive Blue 19 (RB19) dye.
  • Kinetic analysis using Michaelis-Menten equation.
  • Site-directed mutagenesis to identify key residues.
  • Crystal structure analysis and resonance Raman spectroscopy.

Main Results:

  • VcDyP exhibited Michaelis-Menten kinetics with kcat = 1.3 ± 0.3 s⁻¹ and Km = 50 ± 20 μM.
  • Optimal activity was observed at pH 4, with conserved residues Asp144 and Arg230 being essential.
  • Identified Tyr129 and Tyr235 as active site residues for dye degradation at low pH.
  • Identified Tyr109 and Tyr133 as sites for intermolecular covalent bond formation at high pH.
  • Demonstrated a pH-dependent switch in the radical transfer pathway, affecting enzyme activity.

Conclusions:

  • VcDyP possesses unique pH-dependent radical transfer mechanisms for dye degradation.
  • The enzyme's activity is modulated by pH, suggesting a role in survival under acidic conditions, such as gastric acid.
  • Understanding VcDyP's mechanism provides insights into bacterial adaptation and enzyme function.