Monosaccharides as O-glycosyl leaving groups from 3-hydroxy amino acids during base-catalyzed elimination

Vercellotti, John R.; Nienaber, Nancy A.; Jen, Chang Ching

doi:10.1016/s0008-6215(00)84895-8

Cited by 18 publications

(3 citation statements)

References 35 publications

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“…A /3-D-glucopyranoside of /V-glycyl-L-serine methylamide, for example, is stable for 24 h at pH 11, 37 °C (Derevitskaya et al, 1967), and the stability of the threonine derivative would be similar (Vercellotti et al, 1970). iV-Acylglucosylamines are also quite stable; tV-(L-aspartyl)-/?-D-glucosylamine shows no degradation after 7 h in 0.5 N NaOH (Marks & Neuberger, 1961).…”

Section: Discussionmentioning

confidence: 99%

Sucrose 6-.alpha.-D-glucosyltransferase from Streptococcus sobrinus: characterization of a glucosyl-enzyme complex

Mooser

Iwaoka²

1989

Biochemistry

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A covalent glucosyl-enzyme was isolated from a quenched reaction of Streptococcus sobrinus sucrose 6-alpha-D-glucosyltransferase and radiolabeled sucrose. No complex was observed with heat-inactivated enzyme or when sucrose was replaced with radiolabeled maltose or glucose. The complex was stable at pH 2 in 1% sodium dodecyl sulfate, 6.0 M urea, and 4.0 M guanidine hydrochloride, but became increasingly labile with increased pH (32-min half-life at pH 7.0). D-Glucose was the exclusive radiolabeled compound identified when all radioactivity was released under mild alkaline conditions. Glucosyl-enzyme hydrolysis rates were linearly dependent on hydroxide ion concentration, giving a second-order rate constant of 2.15 x 10(5) M-1 min-1. When compared to the base lability of known glycosyl amino acid derivatives, the pH dependency of the glucosyl-enzyme most closely paralleled a glucosyl linkage to a carboxyl group. A novel application of a carbohydrate high-performance liquid chromatography column in aqueous solution was used to identify the anomeric form of D-glucose released on (i) alkaline hydrolysis of denatured glucosyl-enzyme and (ii) native enzyme hydrolysis of sucrose. The beta-anomer was identified in the former case and the alpha-anomer in the latter. The results with the denatured glucosyl-enzyme are consistent with a beta-glucosyl ester linkage to an aspartic or glutamic acid that hydrolyzes at the ester carbon with retention of anomeric configuration; for native glucosyltransferase catalysis, the data are consistent with a beta-glucosyl covalent intermediate as well, where deglucosylation occurs by attack at the acetal carbon with anomeric inversion.(ABSTRACT TRUNCATED AT 250 WORDS)

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Section: Discussionmentioning

confidence: 99%

Sucrose 6-.alpha.-D-glucosyltransferase from Streptococcus sobrinus: characterization of a glucosyl-enzyme complex

Mooser

Iwaoka²

1989

Biochemistry

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“…Inspection of the spectrum at 50 °C of ,2 in which the carbohydrate-attached Thr residue is no longer at the N-terminal position, reveals likewise the Thr-linked GalNAc H-l resonance at 8 4.973 ppm and the Ser-linked GalNAc H-l signal at 8 4.926 ppm. Furthermore, on the basis of the *H NMR data for the structurally related model glycopeptides reported in the literature, perBzlGlcal-Ser(Ar-2,4-dinitrophenyl) methyl ester (6 4.87 ppm) vs. perBzlGlcal -Thr(Ar-2,4-dinitrophenyl) methyl ester (5 5.05 ppm) (Vercellotti et al, 1970) and Fucal-Ser (8 4.88 ppm) vs. Fucal-1 Thr (5 5.05 ppm) (Matsue & Majima, 1983), we can safely assign the upfield resonance to the GalNAcal-*Ser anomeric proton and the downfield resonance to the GalNAcal -Thr anomeric proton. Thus, the chemical shifts 8 4.97-5.01 ppm and 8 4.92-4.94 ppm can be used as diagnostic values for determination of the linkage amino acid in the mucin-type glycopeptides.…”

Section: Discussionmentioning

confidence: 99%

Evidence for unique homologous peptide sequences around the glycosylated seryl and threonyl residues in polysialoglycoproteins isolated from the unfertilized eggs of the Pacific salmon Oncorhynchus keta

Shimamura¹,

Inoue²,

Inoue³

1985

Biochemistry

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Structures of glycopeptides obtained by exhaustive Pronase digestion of high molecular weight (1.7 X 10(5)) salmon egg polysialoglycoprotein have been elucidated. Six principal glycopeptides isolated by gel chromatography and DEAE-Sephadex A-25 chromatography in the absence or presence of borate ion were analyzed for their carbohydrate and amino acid composition, as well as amino acid sequence, and found to be of two distinct types: glycotripeptides, Thr*-Ser*-Glu, and glycotetrapeptides, Thr*-Gly-Pro-Ser, where an asterisk indicates the amino acid residues to which either the Gal beta 1----3GalNAc or Fuc alpha 1----3GalNAc beta 1----3Gal beta 1----4Gal beta 1----3GalNAc chain is attached. Their final yield corresponds to 64% of the original desialylated glycoprotein. In view of the simple amino acid composition of salmon egg polysialoglycoprotein (molar ratio Asp2Thr2Ser3Glu1Pro1Gly1Ala3) and the result of alkaline beta-elimination indicating three carbohydrate units linked to two of two threonine and one of three serine residues, a unique primary structure comprising repetitive sequences of the above two types of glycopeptides, which are interspersed by short nonglycosylated peptides consisting of alanine and aspartic acid, has been proposed for the core protein. The molecular secondary ion mass spectra of underivatized glycopeptides were used to obtain their structural information. The anomeric configuration of the proximal sugar-peptide linkages was proven to be alpha by proton nuclear magnetic resonance spectroscopy. This is the first systematic reported study of O-glycosidically linked glycopeptides by these instrumental methods.

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“…It has been demonstrated that the nature of the eliminated group from substituted 3-hydroxyamino acids was not a primary rate-determining factor and the additional methyl group on threonine has relatively little effect on the rate of ß elimination (Vercellotti et al, 1970). In general, for ß elimination of seryl and threonyl residues to take place at a significant rate it is essential that the amino and carboxyl group be substituted (Derevitskaya et al, 1967).…”

Section: Discussionmentioning

confidence: 99%

β Elimination and sulfite addition as a means of localization and identification of substituted seryl and threonyl residues in proteins and proteoglycans

Simpson¹,

Hranisavljevic²,

Davidson³

1972

Biochemistry

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Monosaccharides as O-glycosyl leaving groups from 3-hydroxy amino acids during base-catalyzed elimination

Cited by 18 publications

References 35 publications

Sucrose 6-.alpha.-D-glucosyltransferase from Streptococcus sobrinus: characterization of a glucosyl-enzyme complex

Sucrose 6-.alpha.-D-glucosyltransferase from Streptococcus sobrinus: characterization of a glucosyl-enzyme complex

Evidence for unique homologous peptide sequences around the glycosylated seryl and threonyl residues in polysialoglycoproteins isolated from the unfertilized eggs of the Pacific salmon Oncorhynchus keta

β Elimination and sulfite addition as a means of localization and identification of substituted seryl and threonyl residues in proteins and proteoglycans

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