6 or alpha1-->3 fucose, under conditions not favorable with existing glycoamidases.
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| Autor: |
Ftouhi-Paquin, N, Hauer, C R, Stack, R F, Tarentino, A L, Plummer, T H |
| Zdroj: |
Journal of Biological Chemistry; September 1997, Vol. 272 Issue: 36 p22960-5, 6p |
| Abstrakt: |
A new glycoamidase, peptide-N4-(N-acetyl-beta-D-glucosaminyl)asparagine amidase (PNGase) At, was discovered in the eukaryote Aspergillus tubigensis. The enzyme was purified to homogeneity, and the DNA sequence was determined by cloning in Escherichia coli. Over 80% of the deduced amino acid sequence was verified independently by Edman analysis and/or electrospray ionization-mass spectrometry of protease fragments of native PNGase At. This glycoamidase contains 12 potential asparagine-linked glycosylation sites, of which at least 9 sites are occupied with typical high mannose oligosaccharides. PNGase At consists of two non-identical glycosylated subunits that are derived from a single polypeptide gene precursor. Evidence is presented suggesting that autocatalysis is involved in subunit formation. PNGase At is an important new tool for analysis of asparagine-linked glycans; it can hydrolyze a broad range of glycopeptides, including those with core-linked alpha1-->6 or alpha1-->3 fucose, under conditions not favorable with existing glycoamidases. |
| Databáze: |
Supplemental Index |
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