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Manipulating intradiol dioxygenases by C-terminus truncation.

Ali Reza Nazmi1, Muralidharan Muthu1, Gareth Lloyd-Jones1

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|March 20, 2019
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Summary

Truncating the C-terminus of intradiol dioxygenases can significantly alter enzyme activity, boosting one enzyme fivefold while reducing others. This protein engineering strategy may enhance biotechnological production of valuable acids.

Keywords:
C-terminusCatechol 1,2-dioxygenaseChlorocatechol 1,2-dioxygenaseTruncation

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Area of Science:

  • Biochemistry
  • Enzymology
  • Microbial Metabolism

Background:

  • Intradiol dioxygenases are key bacterial enzymes in aerobic aromatic compound degradation.
  • Some intradiol dioxygenases possess a longer C-terminus (13-18 amino acids) not conserved in structural models.

Purpose of the Study:

  • To investigate the impact of C-terminal truncation on intradiol dioxygenase activity.
  • To explore protein engineering strategies for enhancing enzyme function.

Main Methods:

  • Protein engineering to create truncated intradiol dioxygenase variants.
  • Enzyme activity assays comparing wild-type and truncated enzymes from *Burkholderia xenovorans* LB400, *Pseudomonas putida* KT2440, and *Acinetobacter baylyi* ADP1.

Main Results:

  • C-terminal truncation altered enzyme activity, increasing LB400 enzyme activity by up to fivefold.
  • Truncation reduced the activity of enzymes from *P. putida* KT2440 and *A. baylyi* ADP1.
  • Observed differences were attributed to variations in amino acid residues contributing to protein stability.

Conclusions:

  • C-terminal truncation is a viable protein engineering strategy to modulate intradiol dioxygenase activity.
  • This approach holds potential for optimizing enzyme function in biotechnological applications, such as muconic and adipic acid production.