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Substrate selectivity in starch polysaccharide monooxygenases.

Van V Vu1, John A Hangasky2, Tyler C Detomasi3

  • 1Nguyen Tat Thanh Hi-Tech Institute, Nguyen Tat Thanh University, Ho Chi Minh City 70000, Vietnam.

The Journal of Biological Chemistry
|June 26, 2019
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Summary
This summary is machine-generated.

Starch-active polysaccharide monooxygenases (AA13 PMOs) preferentially bind and oxidize helical amylose. These enzymes show unique interactions with starch substrates, impacting polysaccharide degradation in biological and industrial settings.

Keywords:
amyloseauxiliary activity (AA) enzymecarbohydrate-binding proteincoppercopper monooxygenasemetalloproteinoxygenasepolysaccharidepolysaccharide monooxygenasestarch

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Area of Science:

  • Biochemistry
  • Enzymology
  • Carbohydrate Chemistry

Background:

  • Polysaccharide degradation is crucial for biological and industrial applications.
  • Starch-active polysaccharide monooxygenases (AA13 PMOs) are enzymes that oxidatively degrade starch.
  • These enzymes hold potential for converting starch into fermentable carbohydrates when used with industrial amylases.

Purpose of the Study:

  • To investigate the oxidative activities of AA13 PMOs from *Neurospora crassa* (*Nc*AA13) and *Myceliophthora thermophila* (*Mt*AA13) on different starch substrates.
  • To analyze the product distribution and binding preferences of these enzymes.
  • To elucidate the structural basis for substrate specificity in AA13 PMOs.

Main Methods:

  • High-performance anion-exchange chromatography coupled with pulsed amperometry detection (HPAEC-PAD) to measure enzyme activity.
  • Analysis of product distribution from enzymatic reactions.
  • Molecular docking studies to identify key residues involved in substrate binding.
  • Enzyme truncation experiments to assess the role of the carbohydrate-binding module.

Main Results:

  • Both *Nc*AA13 and *Mt*AA13 exhibited significantly higher oxidative activity on amylose compared to amylopectin and cornstarch.
  • Product analysis indicated preferential oxidation of glycosidic linkages at specific intervals on the amylose helix.
  • Docking studies and truncation experiments revealed that the active site's shallow groove favors helical amylose binding, even when the carbohydrate-binding module is removed.

Conclusions:

  • AA13 PMOs demonstrate a clear preference for binding and oxidizing the helical starch substrate, amylose.
  • The specific product distributions suggest unique enzymatic interactions with starch substrates.
  • These findings enhance our understanding of enzymatic starch degradation and its potential industrial applications.