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Disaccharide phosphorylases: Structure, catalytic mechanisms and directed evolution.

Shangshang Sun1, Chun You1,2,3

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Disaccharide phosphorylases (DSPs) are versatile enzymes that convert table sugar into valuable products. Protein engineering aims to expand their capabilities for novel glycoside synthesis.

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Area of Science:

  • Enzymology and biocatalysis
  • Carbohydrate chemistry
  • Protein engineering

Background:

  • Disaccharide phosphorylases (DSPs) are carbohydrate-active enzymes with significant potential for biocatalysis.
  • These enzymes are structurally and mechanistically related to glycoside hydrolases and glycosyltransferases.
  • DSPs exhibit high stereo- and regiospecificity, making them suitable for targeted synthesis.

Purpose of the Study:

  • To review the characteristics and classifications of reported DSPs.
  • To summarize the glycoside products synthesized using DSPs.
  • To highlight the ongoing efforts in protein engineering to enhance DSP functionality.

Main Methods:

  • Literature review of characterized disaccharide phosphorylases.
  • Analysis of enzyme structures and mechanisms.
  • Survey of protein engineering strategies applied to DSPs.

Main Results:

  • DSPs are modular enzymes forming active homo-oligomers.
  • Their specificity allows for the synthesis of defined disaccharides.
  • Protein engineering is actively broadening substrate specificities and improving industrial applicability.

Conclusions:

  • Disaccharide phosphorylases are powerful biocatalysts for synthesizing valuable glycosides from common sugars.
  • Ongoing protein engineering efforts are creating a versatile toolbox of DSP catalysts for glycoside synthesis.
  • Further research will expand the industrial applications of these enzymes.