Chain elongation of pectic β-(1→4)-galactan by a partially purified galactosyltransferase from soybean (Glycine max Merr.) hypocotyls

Konishi, Tenji; Kotake, Toshihisa; Tsumuraya, Yoichi

doi:10.1007/s00425-007-0505-3

Cited by 10 publications

(13 citation statements)

References 26 publications

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“…Using a similar fluorometric assay, microsomal soybean GalT activity levels reached approximately 870 pmol min 21 mg 21 protein (Konishi et al, 2007). This implies either that developing compression wood has a higher level of GalT than soybean or that galactan formation is not hindered in pine as compared with soybean.…”

Section: Characterization Of a B(14)-galactan-specific Galt Activitymentioning

confidence: 91%

“…The GalT reaction products from various incubations (1-21 h) were hydrolyzed with endo-b-(1,4)-galactanase (Konishi et al, 2007), leading to only Gal 2 and Gal 3 at completion. Both the acceptor substrate and enzyme-mediated galactan oligomers hydrolyzed to the same end product (Gal 2-3 ; Fig.…”

Section: Biochemical Characterization Of Pine Galt and Analysis Of Enmentioning

confidence: 99%

“…8). This result demonstrated that the Gal incorporation by the GalT activity was via successive b(1,4)-linkage additions at the nonreducing end of the b(1,4)-galactooligosaccharide substrate (Ishii et al, 2004;Konishi et al, 2007). The identity of a subset of enzymatic transfer products from a short incubation was further investigated using ESI-MS, but the analytical cutoff at a mass-to-charge ratio (m/z) of 2,000 prohibited the analysis of larger oligosaccharides.…”

Section: Biochemical Characterization Of Pine Galt and Analysis Of Enmentioning

confidence: 99%

“…Merr.) was only able to extend a few Gal residues in microsomal preparations (Konishi et al, 2007). After further purification, the soybean GalT increased its ability to extend the Gal 7 acceptor, reaching a DP of 40 after the reaction was repeatedly spiked with additional enzyme over a period of 30 h (Konishi et al, 2007).…”

Section: Characterization Of a B(14)-galactan-specific Galt Activitymentioning

confidence: 99%

“…Despite substantial efforts to characterize the biosynthesis of this polymer, b(1,4)-galactan biosynthetic enzymes and their corresponding genes are currently unknown (Peugnet et al, 2001;Geshi et al, 2002Geshi et al, , 2004Abdel-Massih et al, 2003;Kato et al, 2003;Ishii et al, 2004;Konishi et al, 2004Konishi et al, , 2007Gorshkova and Morvan, 2006). However, based on other cell wall polysaccharide biosynthetic enzymes, it is likely that the enzymes involved in the biosynthesis of b(1,4)-galactan are either Golgi localized or pass through the Golgi in transit to the apoplastic space (Reyes and Orellana, 2008).…”

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confidence: 99%

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Exploring the Ultrastructural Localization and Biosynthesis of β(1,4)-Galactan in Pinus radiata Compression Wood

et al. 2009

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Softwood species such as pines react to gravitropic stimuli by producing compression wood, which unlike normal wood contains significant amounts of b(1,4)-galactan. Currently, little is known regarding the biosynthesis or physiological function of this polymer or the regulation of its deposition. The subcellular location of b(1,4)-galactan in developing tracheids was investigated in Pinus radiata D. Don using anti-b(1,4)-galactan antibodies to gain insight into its possible physiological role in compression wood. b(1,4)-Galactan was prominent and evenly distributed throughout the S2 layer of developing tracheid cell walls in P. radiata compression wood. In contrast, b(1,4)-galactan was not detected in normal wood. Greatly reduced antibody labeling was observed in fully lignified compression wood tracheids, implying that lignification results in masking of the epitope. To begin to understand the biosynthesis of galactan and its regulation, an assay was developed to monitor the enzyme that elongates the b(1,4)-galactan backbone in pine. A b(1,4)-galactosyltransferase (GalT) activity capable of extending 2-aminopyridine-labeled galacto-oligosaccharides was found to be associated with microsomes. Digestion of the enzymatic products using a b(1,4)-specific endogalactanase confirmed the production of b(1,4)-galactan by this enzyme. This GalT activity was substantially higher in compression wood relative to normal wood. Characterization of the identified pine GalT enzyme activity revealed pH and temperature optima of 7.0 and 20°C, respectively. The b(1,4)-galactan produced by the pine GalT had a higher degree of polymerization than most pectic galactans found in angiosperms. This observation is consistent with the high degree of polymerization of the naturally occurring b(1,4)-galactan in pine.

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Section: Characterization Of a B(14)-galactan-specific Galt Activitymentioning

confidence: 91%

Section: Biochemical Characterization Of Pine Galt and Analysis Of Enmentioning

confidence: 99%

Section: Biochemical Characterization Of Pine Galt and Analysis Of Enmentioning

confidence: 99%

Section: Characterization Of a B(14)-galactan-specific Galt Activitymentioning

confidence: 99%

mentioning

confidence: 99%

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Exploring the Ultrastructural Localization and Biosynthesis of β(1,4)-Galactan in Pinus radiata Compression Wood

et al. 2009

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Analysis of carbohydrates and glycoconjugates by matrix‐assisted laser desorption/ionization mass spectrometry: An update for 2007–2008

Harvey

2011

Mass Spectrometry Reviews

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This review is the fifth update of the original review, published in 1999, on the application of MALDI mass spectrometry to the analysis of carbohydrates and glycoconjugates and brings coverage of the literature to the end of 2008. The first section of the review covers fundamental studies, fragmentation of carbohydrate ions, use of derivatives and new software developments for analysis of carbohydrate spectra. Among newer areas of method development are glycan arrays, MALDI imaging and the use of ion mobility spectrometry. The second section of the review discusses applications of MALDI MS to the analysis of different types of carbohydrate. Specific compound classes that are covered include carbohydrate polymers from plants, N- and O-linked glycans from glycoproteins, biopharmaceuticals, glycated proteins, glycolipids, glycosides and various other natural products. There is a short section on the use of MALDI mass spectrometry for the study of enzymes involved in glycan processing and a section on the use of MALDI MS to monitor products of the chemical synthesis of carbohydrates with emphasis on carbohydrate-protein complexes and glycodendrimers. Corresponding analyses by electrospray ionization now appear to outnumber those performed by MALDI and the amount of literature makes a comprehensive review on this technique impractical. However, most of the work relating to sample preparation and glycan synthesis is equally relevant to electrospray and, consequently, those proposing analyses by electrospray should also find material in this review of interest.

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The structure, function, and biosynthesis of plant cell wall pectic polysaccharides

Caffall

Mohnen

2009

Carbohydrate Research

1,343

892

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Chain elongation of pectic β-(1→4)-galactan by a partially purified galactosyltransferase from soybean (Glycine max Merr.) hypocotyls

Cited by 10 publications

References 26 publications

Exploring the Ultrastructural Localization and Biosynthesis of β(1,4)-Galactan in Pinus radiata Compression Wood

Exploring the Ultrastructural Localization and Biosynthesis of β(1,4)-Galactan in Pinus radiata Compression Wood

Analysis of carbohydrates and glycoconjugates by matrix‐assisted laser desorption/ionization mass spectrometry: An update for 2007–2008

The structure, function, and biosynthesis of plant cell wall pectic polysaccharides

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