1991
DOI: 10.1111/j.1432-1033.1991.tb16166.x
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Peptide‐N4‐(N‐acetyl‐β‐glucosaminyl)asparagine amidase F cannot release glycans with fucose attached α1 → 3 to the asparagine‐linked N‐acetylglucosamine residue

Abstract: The ability of peptide‐N4‐(N‐acetyl‐β‐glucosaminyl)asparagine amidase F (PNGase F) from Flavobacterium meningosepticum and PNGase A from sweet almonds to deglycosylate N‐glycopeptides and N‐glycoproteins from plants was compared. Bromelain glycopeptide and horseradish peroxidase‐C glycoprotein, which contain xylose linked β1 → 2 to β‐mannose and fucose linked α1 → 3 to the innermost N‐acetylglucosamine, were used as substrates. In contrast to PNGase A, the enzyme from F. meningosepticum did not act upon these … Show more

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Cited by 392 publications
(251 citation statements)
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“…PNGase F cleaves off the intact glycan as glycosylamine, which is readily converted to regular glycan. With few exceptions, PNGase F releases practically all protein-bound N-linked carbohydrates except those with fucose attached to the third position of the Asn-linked GlcNAc residue 12 . Their corresponding glycoproteins are commonly found in plants and in nematodes.…”
Section: Release Of Glycansmentioning
confidence: 99%
“…PNGase F cleaves off the intact glycan as glycosylamine, which is readily converted to regular glycan. With few exceptions, PNGase F releases practically all protein-bound N-linked carbohydrates except those with fucose attached to the third position of the Asn-linked GlcNAc residue 12 . Their corresponding glycoproteins are commonly found in plants and in nematodes.…”
Section: Release Of Glycansmentioning
confidence: 99%
“…Both N-glycosidase F and N-glycosidase A cleave the bond between N-linked glucosamine in the glycan and asparagine in glycoproteins and convert this residue to aspartic acid [13]. N-Glycosidase A has broader specificity than N-glycosidase F in that the former can release oligosaccharides containing core fucosylation at C-3 of the N-glucosamine residue attached to asparagine, whereas the latter cannot [14]. Endoglycosidase F hydrolyzes the glycosidic bond of the penultimate N-acetylglucosamine leaving the ultimate amino sugar (glucosamine) attached to asparagine, provided that this residue is not fucosylated.…”
Section: Identification Of the Glycosylation Sites In Gp-iimentioning
confidence: 99%
“…As a test for the presence of N-glycans, rose CM-AGPs were treated with glycoamidase A, which cleaves a broader range of substrates than glycoamidase F (38). For example, plant glycoproteins with N-glycans containing Fuc linked ␣1 3 3 to the innermost GlcNAc are cleaved by glycoamidase A but are highly resistant to glycoamidase F (39). No evidence of loss of Man and GlcN relative to other sugars was observed when CM-AGPs were treated with glycoamidase A, whereas 47% of the Man and GlcN were lost when ribonuclease B was treated with glycoamidase A under the same conditions (data not shown).…”
Section: Table III Chemical Analysis Of Glycolipids Copurifying With mentioning
confidence: 99%