Deglycosylating Enzymes Acting on N-glycans in Fungi: Insights From a Genome Survey

Biochim Biophys Acta Gen Subj. 2017 Nov;1861(11 Pt A):2551-2558. doi: 10.1016/j.bbagen.2017.08.022. Epub 2017 Sep 7.

Abstract

Background: N-Glycosylation, one of the most prominent post-translational modifications of proteins, is found in all domains of life, i.e. eukaryotes, bacteria and archaea, and has been shown to play a crucial role in modulating the physicochemical/physiological properties of carrier proteins. Deglycosylating enzymes that act on N-glycans are widely used in analyzing the structures/functions of N-glycans. Fungi are known to produce various deglycosylating enzymes, some of which are fungi-specific. While such enzymes likely are biologically relevant in fungal biology, their properties as well as their functions have not been explored in detail.

Scope of review: In this review, we summarize the current knowledge of fungal deglycosylating enzymes and discuss their biological significance.

Major conclusions: As of this writing, five types of deglycosylating enzymes that act on N-glycans are known to occur in fungi; (1) the cytosolic peptide: N-glycanase (PNGase), (2) the acidic PNGase, (3) the glycoside hydrolase family (GH) 85 endo-β-N-acetylglucosaminidase (ENGase), (4) the GH18 cytosolic ENGase, and (5) the GH18 secreted ENGase. Interestingly, genome surveys indicate that the loss of cytosolic PNGase activity in certain fungi coincide with the occurrence of GH18 cytosolic ENGase, implying that the GH18 ENGase serves to replace the deglycosylation function of the cytosolic PNGase in those filamentous ascomycete fungi.

General significance: Our review concludes that fungi promise to be valuable organisms for developing an understanding of the biological functions of PNGases/ENGases.

Keywords: Deglycosylation; Endo-β-N-acetylglucosaminidase; Fungi; GH18; GH85; Peptide: N-glycanase.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Fungi / chemistry
  • Fungi / enzymology*
  • Genome, Fungal*
  • Glycosylation*
  • Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase / chemistry
  • Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase / chemistry
  • Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase / genetics
  • Polysaccharides / chemistry
  • Polysaccharides / metabolism*
  • Protein Processing, Post-Translational / genetics

Substances

  • Polysaccharides
  • Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase
  • Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase