Peptide‐N4‐(N‐acetyl‐β‐glucosaminyl)asparagine amidase F cannot release glycans with fucose attached α1 → 3 to the asparagine‐linked N‐acetylglucosamine residue

Tretter, Verena; Altmann, Friedrich; März, Leopold

doi:10.1111/j.1432-1033.1991.tb16166.x

Cited by 388 publications

(251 citation statements)

References 31 publications

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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%

Analysis of protein glycosylation by mass spectrometry

2007

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We present a detailed protocol for the structural analysis of protein-linked glycans. In this approach, appropriate for glycomics studies, N-linked glycans are released using peptide N-glycosidase F and O-linked glycans are released by reductive alkaline b-elimination. Using strategies based on mass spectrometry (matrix-assisted laser desorption/ionization-time of flight mass spectrometry and nano-electrospray ionization mass spectrometry/mass spectrometry (nano-ESI-MS-MS)), chemical derivatization, sequential exoglycosidase digestions and linkage analysis, the structures of the N-and/or O-glycans are defined. This approach can be used to study the glycosylation of isolated complex glycoproteins or of numerous glycoproteins encountered in a complex biological medium (cells, tissues and physiological fluids).

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Section: Release Of Glycansmentioning

confidence: 99%

Analysis of protein glycosylation by mass spectrometry

2007

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“…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%

Amino‐acid sequence and glycan structures of cysteine proteases with proline specificity from ginger rhizome Zingiber officinale

Choi

Laursen

2000

European Journal of Biochemistry

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The ginger proteases (GP-I and GP-II), isolated from the ginger rhizome Zingiber officinale, have an unusual substrate specificity preference for cleaving peptides with a proline residue at the P 2 position. The complete amino-acid sequence of GP-II, a glycoprotein containing 221 amino acids, and about 98% that of GP-I have been determined. Both proteases, which are 82% similar, have cysteine residues at positions 27 and histidines at position 161, corresponding to the essential cysteine±histidine diads found in the papain family of cysteine proteases, and six corresponding cysteine residues that form the three invariant disulfide linkages seen in this family of proteins. The sequence homology with other members (papain, bromelain, actinidin, protease omega, etc.) of this family is < 50%. GP-II has two predicted glycosylation sites at Asn99 and Asn156. Analyisis by electrospray and collision-induced dissociation MS showed that both sites were occupied by the glycans (Man) 3 (Xyl) 1 (Fuc) 1 (GlcNAc) 2 and (Man) 3 (Xyl) 1 (Fuc) 1 (GlcNAc) 3 , in a ratio of < 7 : 1. Both glycans are xylose containing biantennary complex types that share the common core structural unit, Man136(Man133) (Xyl132)Man134GlcNAc134(Fuc133)GlcNAc for the major form, with an additional N-acetylglucosamine residue being linked, in the minor form, to one of the terminal mannose units of the core structure.Keywords: amino-acid sequence; cysteine protease; ginger; glycoprotein; glycosylation site; proline peptidase; proteinase; mass spectrometry. Some 20 families of peptidases dependent on a cysteine residue at the active center are known [1]. The most prominent of these is the papain family, which includes peptidases with a wide variety of activities, including endopeptidases with broad specificity (e.g. papain) and narrow specificity (glycyl endopeptidase), amino peptidases, and a dipeptidyl peptidase. Enzymes of the papain family are found in a wide variety of life forms: baculovirus, eubacteria, yeast, probably all protozoa, plants and animals. Papain homologs are generally either lysosomal (vacuolar) or secreted proteins. In plants, they are found in the vacuoles, but also extracellularly, as in the latex of papaya or fig. Plant cysteine proteinases include papain from papaya (Carica papaya), bromelain from pineapple stem and actinidin from the Chinese gooseberry or kiwi fruit (Actinidia chinensis) [1].Ginger proteases from ginger rhizome, Zingiber officinale, were first reported by Ichikawa et al.[2] in 1973. Two proteases, designated GP-I and GP-II were isolated by chromatography on DEAE-cellulose and tentatively classified as cysteine proteases based on their inhibition by thiol reagents and their relative molecular masses, estimated at < 22 500 by gel filtration. More recently, these proteases were separated as mercuribenzoate derivatives into three fractions by IEF [3]. It has been reported [4] that these proteases have both proteinase and collagenase activities; ginger root extracts have also been tested as a meat tenderizer [5,6].Rec...

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“…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%

Presence of a Glycosylphosphatidylinositol Lipid Anchor on Rose Arabinogalactan Proteins

Svetek¹,

Yadav

Nothnagel

1999

Journal of Biological Chemistry

135

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Arabinogalactan proteins constitute a class of plant cell surface proteoglycans with widespread occurrence and suggested functions in various aspects of plant growth and development, including cell proliferation, expansion, marking, and death. Previous investigations of subcellular fractions from suspension-cultured cells of "Paul's Scarlet" rose (Rosa sp.) have revealed extensive structural similarity between some soluble arabinogalactan proteins from the cell wall space and some plasma membrane-associated arabinogalactan proteins, thus inspiring the present investigation of the mechanism through which these inherently water-soluble molecules are held on the plasma membrane. Several lines of evidence gained through a combination of methods including reversed-phase chromatography, treatment with phosphatidylinositol-specific phospholipase C, and chemical structural analysis now show that some rose arabinogalactan proteins carry a ceramide class glycosylphosphatidylinositol lipid anchor. The predominant form of the ceramide is composed of tetracosanoic acid and 4-hydroxysphinganine. Plasma membrane vesicles readily shed arabinogalactan proteins by an inherent mechanism that appears to involve a phospholipase. This finding has significance toward understanding the biosynthesis, localization, and function of arabinogalactan proteins and toward stimulating other studies that may expand the currently very short list of higher plant proteins found to carry such membrane lipid anchors.

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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

Cited by 388 publications

References 31 publications

Analysis of protein glycosylation by mass spectrometry

Analysis of protein glycosylation by mass spectrometry

Amino‐acid sequence and glycan structures of cysteine proteases with proline specificity from ginger rhizome Zingiber officinale

Presence of a Glycosylphosphatidylinositol Lipid Anchor on Rose Arabinogalactan Proteins

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