PlumX Metrics
Embed PlumX Metrics

Elicitation of an oxidase activity in bacterial luciferase by site-directed mutation of a noncatalytic residue.

Journal of Biological Chemistry, ISSN: 0021-9258, Vol: 265, Issue: 8, Page: 4200-4203
1990
  • 26
    Citations
  • 0
    Usage
  • 2
    Captures
  • 0
    Mentions
  • 0
    Social Media
Metric Options:   Counts1 Year3 Year

Metrics Details

  • Citations
    26
    • Citation Indexes
      26
      • CrossRef
        26
  • Captures
    2

Abstract Description

Flavin-dependent external monooxygenases and oxidases could catalyze the same flavin oxidation reaction involving distinct mechanisms. To gain insights into enzyme structure-function relationship, site-directed mutagenesis was carried out for Vibrio harveyi luciferase, a monooxygenase. The substitution of the alpha subunit cysteine 106 by alanine shows unambiguously that the alphaCys106 is not essential to catalysis. The corresponding substitution by valine resulted in a substantial reduction of the bioluminescence activity correlatable with the induction of a new flavin oxidation activity typical for oxidases. These findings indicate that mutation of a single noncatalytic residue at the active center of a flavoenzyme could transform one enzyme type to another, thus highlighting the subtlety of enzyme active site structure in relation to catalysis and the versatility of enzyme evolution.

Provide Feedback

Have ideas for a new metric? Would you like to see something else here?Let us know