Molecular cloning, expression, and characterization of a novel endo-alpha-N-acetylgalactosaminidase from Enterococcus faecalis

Biochemical and Biophysical Research Communications
Hatsumi M GodaMakoto Ito

Abstract

We report here the molecular cloning, expression and characterization of a novel endo-alpha-N-acetylgalactosaminidase, classified into the GH101 family, from Enterococcus faecalis (endo-EF). The recombinant endo-EF was found to catalyze the liberation of core1-disaccharides (Galbeta1-3GalNAc) from core1-pNP (Galbeta1-3GalNAcalpha-pNP) like other GH101 family enzymes. However, endo-EF seems to differ in specificity from the GH101 enzymes reported to date, because it was able to release trisaccharides from core2-pNP (Galbeta1-3[GlcNAcbeta1-6]GalNAcalpha-pNP) and tetrasaccharides from Gal-core2-pNP (Galbeta1-3[Galbeta1-3GlcNAcbeta1-6]GalNAcalpha-pNP). Interestingly, the enzyme could transfer not only core1-disaccharides but also core2-trisaccharides to alkanols generating alkyl-oligosaccharides. Endo-EF should facilitate O-glycoprotein research.

References

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Citations

Jan 12, 2012·Applied Microbiology and Biotechnology·Coraline RigouinMichel Dion
Oct 21, 2010·Glycobiology·Tongzhong JuRichard D Cummings
Oct 24, 2014·Future Microbiology·Jonathan Sjögren, Mattias Collin
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Dec 12, 2017·Mass Spectrometry Reviews·Qiwei ZhangJianjun Li
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May 30, 2017·Chemical Science·David Lim, Antony J Fairbanks
Jul 27, 2021·ACS Chemical Biology·Jacob F WardmanStephen G Withers
Oct 16, 2021·Scientific Reports·Zhengliang L Wu, James M Ertelt

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