A 500-MHz1H-NMR study on theN-linked carbohydrate chain of bromelain

Vliegenthart, Johannes F.G.; Kuik, J. Albert van; Hoffmann, Rainer A.; Mutsaers, Johanna H. G. M.; Halbeek, Herman van; Kamerling, Johannis P.

doi:10.1007/bf01108609

Cited by 63 publications

(64 citation statements)

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“…4. In both cases the difference in mass between the glycosylated and nonglycosylated peptides is < 1170, which which is close to the mass of the glycan found in the homologous cysteine protease, bromelain, which contains three hexose, two pentose and two N-acetylhexosamine residues [15,16].…”

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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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 structures of many oligosaccharides in plant glycoproteins have been elucidated during the last decade [3 -141. These works have revealed that xylose-containing oligosaccharides are widely distributed throughout the plant kingdom, although, xylose-containing N-linked oligosaccharides were also found in glycoproteins from gastropods [15, 161 and Chlorophyceae [17]. The biosynthesis of the oligosaccharide chains in plant glycoproteins has been recently investigated…”

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confidence: 99%

Studies on synthetic pathway of xylose‐containing N‐linked oligosaccharides deduced from substrate specificities of the processing enzymes in sycamore cells (Acer pseudoplatanus L.)

Tezuka

Hayashi

Ishihara

et al. 1992

European Journal of Biochemistry

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We measured the activities of a-I ,3-mannosyl-glycoprotein ~-l,2-N-acetylglucosaminyltransferase, a-1,6-mannosyl-glycoprotein p-1,2-N-acetylglucosaminyltransferase, ~-3,4-mannosyl-glycoprotein p-1,2-xylosyltransferase and glycoprotein 3-a-~-fucosyltransferase in the Golgi fraction of suspension-cultured cells of sycamore (Acer pseudoplatanus L.) using fluorescence-labelled oligosaccharides as acceptor substrates for these transferase reactions. The structures of the pyridylaminated oligosaccharides produced by these reactions were analyzed by two-dimensional sugar mapping using high-performance liquid chromatography. We demonstrated that The biosynthesis of oligosaccharides in animal cells has been well characterized [l]. This pathway starts from the transfer of Glc3Man9GlcNAc, to nascent polypeptide chains in the endoplasmic reticulum. The processing of Glc3Man9GlcNAcz begins with the removal of three glucose and four mannose residues by sequential reactions of a-glucosidases and aCorrespondence to N . Takahashi, Nagoya City University, College of Nursing, Mizuho-ku, Nagoya, Japan 467.Abbreviations. GlcNAc transferase I, a-I ,3-mannosyl-glycoprotcin ~-1,2-N-acetyIglucosaminyltransferase; GlcNAc transferase 11, a-1,6-mannosyl-glycoprotein ~-1,2-N-acetylglucosaminyltransferase; xylosyl transferase, ~-1,4-mannosyl-glycoprotein B-1,2-xylosyltransferase; fucosyl transferase, glycoprotein 3-a-~-fucosyltransferase; Fuc, fucose; UDP-Xyl, uridine(5')diphospho(l)-/?-xylose; GDP-Fuc, guanosine(5')diphospho-a-L-fucose.Enzymes. a-l,3-Mannosyl-glycoprotein ~-1,2-N-acetylglucosami- mannosidases. The product of these reactions, Man5-GlcNAc,, is the precursor of all N-acetyllactosamine-type oligosaccharides [2]. It is the substrate of GlcNAc transferase I which produces the first N-acetyllactosamine-type intermediate, GlcNAcMan,GlcNAcz. Various N-acetyllactosamine-type oligosaccharides found in animal glycoproteins are produced from GlcNAcMan5GlcNAcz after further modification by a-mannosidase 11, GlcNAc transferase, fucosyl transferase, galactosyl transferase and sialyl transferase. The structures of many oligosaccharides in plant glycoproteins have been elucidated during the last decade [3 -141. These works have revealed that xylose-containing oligosaccharides are widely distributed throughout the plant kingdom, although, xylose-containing N-linked oligosaccharides were also found in glycoproteins from gastropods [15, 161 and Chlorophyceae [17]. The biosynthesis of the oligosaccharide chains in plant glycoproteins has been recently investigatedThe biosynthesis of N-linked oligosaccharide in rice xamylase containing GlcNAc,Man3XylGlcNAcz has been par-

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“…These crossreactive glycans were designated 'Crossreactive Carbohydrate determinants' or CCDs (Aalberse et al, 1981a,b). The structure of some strongly immunogenic crossreactive non-mammalian glycans has been elucidated (Ishihara et al, 1979;Kaladas et al, 1983;Van Kuik et al, 1986;D'Andrea et al, 1988;Faye and Chrispeels, 1988;Hayashi et al, 1990;Prenner et al, 1992;Staudacher et al, 1992;Driouich et al, 1993;Faye et al, 1993) and for selected antibodies differences in immune reactivity have been found to depend on a fucose and a xylose.…”

Section: What Is Special About Vegetable Glycoproteinsmentioning

confidence: 99%

Food allergens

Aalberse

1997

Environmental Toxicology and Pharmacology

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A food allergen may be defined as a substance that reacts with IgE antibodies, induces allergic sensitisation or induces allergic reactions. Some allergens only induce allergic sensitisation but do not provoke symptoms, while others bind IgE but do not induce mast cell degranulation. There is no common structure that can predict whether a given antigen may be a strong food allergen. A complete food allergen, e.g. fish parvalbumin, is capable of stimulating the immune system to produce IgE antibodies, and degranulate mast cells upon subsequent contact. The reason(s) for why some patients with IgE to ovalbumin tolerate eggs, and why some react on one occasion but not on another, are mostly unclear, but may be related to changes in gut permeability induced by other food substances or by gastro-intestinal inflammation prior to the allergen contact. IgE antibodies to fruit or vegetables often show cross-reactivity, due to carbohydrate structures. These cross-reactive glycans have been designated cross-reactive carbohydrate determinants (CCD). Anti-CCD antibodies are highly cross-reactive. The antibodies do not have clinical significant because CCD-containing foods are usually well-tolerated by patients with IgE antibodies to CCD. These IgE antibodies may cause confusion in relation to allergy diagnosis. © 1997 Elsevier Science B.V.

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A 500-MHz1H-NMR study on theN-linked carbohydrate chain of bromelain

Cited by 63 publications

References 17 publications

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

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

Studies on synthetic pathway of xylose‐containing N‐linked oligosaccharides deduced from substrate specificities of the processing enzymes in sycamore cells (Acer pseudoplatanus L.)

Food allergens

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