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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Chemical Compound Review: 

AC1MIYYA     (2S)-2-[[(2R,3R,4R,5R,6R)-3- acetamido-4...

Synonyms: M-5 Gna-2 asn, 38784-68-8, (Man)5(glcnac)2Asn
 
 
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High impact information on M-5 Gna-2 asn

  • Comparison of the relative rates of hydrolysis of these compounds with (Man)5(GlcNAc)2-Asn, the most active substrate to date for the endoglycosidase, revealed (Man)4(GlcNAc)2Asn to be hydrolyzed faster than (Man)5(GlcNAc)2Asn and (Man)3-(GlcNAc)2Asn to be equal to or slightly better than (Man)5(GlcNAc)2Asn as a substrate [1].
  • Heterogeneities of the two ovalbumin glycopeptides, (Man)5(GlcNAc)2Asn and (Man)6(GlcNAc)2Asn, were revealed by borate paper electrophoresis of oligosaccharide alcohols obtained from the glycopeptides by endo-beta-N-acetylglucosaminidase H digestion and NaB3H4 reduction [2].

References

  1. Asparaginyl glycopeptides with a low mannose content are hydrolyzed by endo-beta-N-acetylglucosaminidase H. Trimble, R.B., Tarentino, A.L., Plummer, T.H., Maley, F. J. Biol. Chem. (1978) [Pubmed]
  2. Structural studies of two ovalbumin glycopeptides in relation to the endo-beta-N-acetylglucosaminidase specificity. Tai, T., Yamashita, K., Ogata-Arakawa, M., Koide, N., Muramatsu, T., Iwashita, S., Inoue, Y., Kobata, A. J. Biol. Chem. (1975) [Pubmed]
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