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Enzyme evolution can be driven by remote loops, not just the active site. A specific loop in glycoside hydrolase family 19 (GH19) chitinase enables new antifungal activity by accessing the fungal cell wall.

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Area of Science:

  • Enzymology
  • Protein Engineering
  • Evolutionary Biology

Background:

  • Protein loops are key to enzyme function evolution.
  • Mechanisms of loop acquisition and new function emergence are poorly understood.
  • Glycoside hydrolase family 19 (GH19) chitinases are vital for plant defense against pathogens.

Purpose of the Study:

  • Investigate the evolutionary mechanisms of loop acquisition in GH19 chitinases.
  • Determine the role of specific loops in acquiring new functions, such as antifungal activity.
  • Understand how remote loops contribute to enzyme function and evolution.

Main Methods:

  • Phylogenetic analysis of GH19 chitinase evolution.
  • Identification and characterization of loop elements.
  • Functional assays to assess enzyme activity, including antifungal properties.
  • Structural analysis to understand intramolecular interactions.

Main Results:

  • A specific loop, distant from the catalytic site, is essential for novel antifungal activity in GH19 chitinases.
  • This remote loop directly interacts with the fungal cell wall.
  • The loop requires a defined structure, stabilized by long-range intramolecular interactions, to function.
  • The original catalytic activity is maintained while acquiring new functions.

Conclusions:

  • Nature utilizes remote loops for acquiring new enzyme functions, like antifungal activity.
  • Specific loop structures stabilized by intramolecular interactions are crucial for novel functions.
  • This strategy allows for functional diversification without compromising existing catalytic activity.
  • Findings offer insights for designing novel enzymes with tailored functions.