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PNGases as valuable tools in glycoprotein analysis
1Glycomics and Glycan Bioengineering Research Center, College of Food Science and Technology, Nanjing Agricultural University, 1 Weigang, Nanjing 210095, P.R. China. josef.voglmeir@njau.edu.cn.
Protein and Peptide Letters
|July 1, 2014
Summary
Peptide-N4-(N-acetyl-α-glucosaminyl) asparagine amidases (PNGases) are crucial enzymes found in prokaryotes and eukaryotes. This review summarizes the properties and applications of three main PNGase types in glycopeptide and glycoprotein analysis.
Area of Science:
- Biochemistry
- Glycobiology
- Enzymology
Background:
- Peptide-N4-(N-acetyl-α-glucosaminyl) asparagine amidases (PNGases) are ubiquitous enzymes found in prokaryotic and eukaryotic organisms.
- PNGases play a role in lysosomal refolding machinery in higher organisms.
- Over 30 eukaryotic and bacterial PNGases have been identified and studied.
Purpose of the Study:
- To review the current knowledge of PNGase structures, properties, and functions.
- To categorize PNGases into three main types: PNGase F-like, acidic PNGases, and cytoplasmic PNGases.
- To discuss the applications of commercially available PNGases in glycopeptide and glycoprotein analysis.
Main Methods:
- Literature review of existing research on PNGases.
- Classification of PNGases based on structural and functional characteristics.
- Analysis of applications in glycopeptide and glycoprotein analysis.
Main Results:
- PNGases can be primarily divided into three distinct types based on their properties.
- Detailed understanding of PNGase F-like, acidic, and cytoplasmic PNGases.
- Commercial PNGases are valuable tools for glycopeptide and glycoprotein analysis.
Conclusions:
- PNGases represent a diverse group of enzymes with significant biological roles.
- The classification into three types aids in understanding their varied functions.
- PNGases are essential for advancing glycopeptide and glycoprotein research and analysis.
