Properties of family 79 β-glucuronidases that hydrolyze β-glucuronosyl and 4-O-methyl-β-glucuronosyl residues of arabinogalactan-protein

Konishi, Tenji; Kotake, Toshihisa; Soraya, Dina; Matsuoka, Koji; Koyama, Tetsuo; Kaneko, Satoshi; Igarashi, Kiyohiko; Samejima, Masahiro; Tsumuraya, Yoichi

doi:10.1016/j.carres.2008.03.004

Cited by 54 publications

(43 citation statements)

References 39 publications

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“…These values of AcGlcA79A are similar to the previously reported values of GH79 enzymes (7). The K m values of the A. niger and N. crassa recombinant GH79 enzymes were 0.030 and 0.038 mM, respectively, and the k cat values were 26.9 and 13.5 s Ϫ1 , respectively (7). Because the A. niger and N. crassa enzymes showed 4-O-methyl-␤-glucuronidase activity, the activity of AcGlcA79A for the MeGlcA-containing oligosaccharide MeGlcA-␤-1,6-Gal 2 was tested.…”

Section: Resultsmentioning

confidence: 98%

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Structural and Biochemical Characterization of Glycoside Hydrolase Family 79 β-Glucuronidase from Acidobacterium capsulatum

Michikawa

Ichinose

Momma

et al. 2012

Journal of Biological Chemistry

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Background:The three-dimensional structures of ␤-glucuronidase have been solved only for the GH2 enzymes. Results: AcGlcA79A is composed of a (␤/␣) 8 -barrel domain and a ␤-domain. Conclusion:The substrate binding site of AcGlcA79A is adapted for recognition of GlcA as a substrate. Significance: This is the first report describing the crystal structure, mechanism, and catalytic residues of a GH79 enzyme.

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Section: Resultsmentioning

confidence: 98%

“…The A. niger and N. crassa enzymes have been shown to release both GlcA and 4-O-methyl-GlcA (MeGlcA) from arabinogalactan proteins (6,7). No GH2 ␤-glucuronidases are known in plants, and no GH2 ␤-glucuronidase homologous sequences have been found in plants (17).…”

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confidence: 99%

Structural and Biochemical Characterization of Glycoside Hydrolase Family 79 β-Glucuronidase from Acidobacterium capsulatum

Michikawa

Ichinose

Momma

et al. 2012

Journal of Biological Chemistry

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“…AGP-Specific Enzymes, b-Galactosyl Yariv Reagent Synthesis, and Preparation of AG Proteins a-L-Arabinofuranosidase (EC 3.2.1.55), exo-b-(1→3)-galactanase (EC 3.2.1.145), b-glucuronidase (EC 3.2.1.31), and endo-b-(1→6)-galactanase (EC 3.2.1.164) were prepared by methods described previously (Tsumuraya et al, 1990;Kotake et al, 2004;Konishi et al, 2008;Takata et al, 2010). Arabidopsis leaf AGPs were prepared using a protocol adapted from Tsumuraya et al (1984aTsumuraya et al ( , 1988.…”

Section: Air Preparationmentioning

confidence: 99%

Structural Characterization of Arabidopsis Leaf Arabinogalactan Polysaccharides

et al. 2012

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Proteins decorated with arabinogalactan (AG) have important roles in cell wall structure and plant development, yet the structure and biosynthesis of this polysaccharide are poorly understood. To facilitate the analysis of biosynthetic mutants, water-extractable arabinogalactan proteins (AGPs) were isolated from the leaves of Arabidopsis (Arabidopsis thaliana) plants and the structure of the AG carbohydrate component was studied. Enzymes able to hydrolyze specifically AG were utilized to release AG oligosaccharides. The released oligosaccharides were characterized by high-energy matrix-assisted laser desorption ionization-collision-induced dissociation mass spectrometry and polysaccharide analysis by carbohydrate gel electrophoresis. The Arabidopsis AG is composed of a b-(1→3)-galactan backbone with b-(1→6)-D-galactan side chains. The b-(1→6)-galactan side chains vary in length from one to over 20 galactosyl residues, and they are partly substituted with single a-(1→3)-Larabinofuranosyl residues. Additionally, a substantial proportion of the b-(1→6)-galactan side chain oligosaccharides are substituted at the nonreducing termini with single 4-O-methyl-glucuronosyl residues via b-(1→6)-linkages. The b-(1→6)-galactan side chains are occasionally substituted with a-L-fucosyl. In the fucose-deficient murus1 mutant, AGPs lack these fucose modifications. This work demonstrates that Arabidopsis mutants in AGP structure can be identified and characterized. The detailed structural elucidation of the AG polysaccharides from the leaves of Arabidopsis is essential for insights into the structure-function relationships of these molecules and will assist studies on their biosynthesis.

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“…When multiple products were detected by HPAEC PAD, the concentration of the product was indicated in total amounts of the multiple products. Upon addition of previously reported preferable acceptors for the enzyme from A. niger such as D glucose, D galactose and D xylose, 3) the enzyme transferred glucuronyl residues to 2 deoxy D glucose, 2 deoxy D galacotse, D glucosamine hydrochloride and D galactosamine hydrochloride. Like D mannose and L arabinose, 3) the products of D allose, D gulose and D mannosamine hydrochloride also were much smaller amounts than that of D glucose.…”

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confidence: 93%

“…1 3) β Glucuronidase from A. niger has been also reported to catalyze glucuronyl transfer to the saccharides with stereochemistry similar to galactose. 3) The transglycosylation products of D galactose has been reported to be β GlcA(1 6)Gal.…”

mentioning

confidence: 99%

Acceptor and Substrate Specificity of .BETA.-Glucuronidase with Transglycosylation Activity from Aspergillus niger

高明¹,

太郎²,

博文³

et al. 2009

J. Appl. Glycosci.

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Properties of family 79 β-glucuronidases that hydrolyze β-glucuronosyl and 4-O-methyl-β-glucuronosyl residues of arabinogalactan-protein

Cited by 54 publications

References 39 publications

Structural and Biochemical Characterization of Glycoside Hydrolase Family 79 β-Glucuronidase from Acidobacterium capsulatum

Structural and Biochemical Characterization of Glycoside Hydrolase Family 79 β-Glucuronidase from Acidobacterium capsulatum

Structural Characterization of Arabidopsis Leaf Arabinogalactan Polysaccharides

Acceptor and Substrate Specificity of .BETA.-Glucuronidase with Transglycosylation Activity from Aspergillus niger

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