Assignment of the 1H and 13C NMR spectra of 2-aminobenzamide-labeled galacto- and arabinooligosaccharides

Ishii, Tadashi; Ono, Hiroshi; Maeda, Ikuko

doi:10.1007/s10086-004-0647-x

Cited by 6 publications

(2 citation statements)

References 11 publications

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“…The resonance of the Araf residue next to the reducing end (residue A) occurs at d5.075. These chemical shift values and the small J 1,2 coupling constants are consistent with the presence of a-linked L-Araf residues (Mizutani et al, 1989;Ishii et al, 2005b). The ring protons of the enzymatically formed Ara 5 -2AB were not assigned because the oligosaccharide was available in limited amounts and its ring proton signals overlapped with the proton signals of the residual Triton X-100.…”

Section: Characterization Of Enzymatically Formed 2ab-labeled Arabinomentioning

confidence: 56%

Identification of a Mung Bean Arabinofuranosyltransferase That Transfers Arabinofuranosyl Residues onto (1, 5)-Linked α-l-Arabino-Oligosaccharides

et al. 2006

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Arabinofuranosyltransferase activity was identified in Golgi membranes obtained from mung bean (Vigna radiata) hypocotyls. The enzyme transfers the arabinofuranosyl (Araf) residue from UDP-b-L-arabinofuranose to exogenous (1, 5)-linked a-L-arabinooligosaccharides labeled at their reducing ends with 2-aminobenzamide. The transferred residue was shown, using 1 H-nuclear magnetic resonance spectroscopy and a-L-arabinofuranosidase treatment, to be a-L-Araf and to be linked to O-5 of the nonreducing terminal Araf residue of the acceptor oligosaccharide. The enzyme was nonprocessive because only a single Araf residue was added to the acceptor molecule. Arabino-oligosaccharides with a degree of polymerization between 3 and 8 were acceptor substrates. The 2-aminobenzamide-labeled arabino-tetra-and pentasaccharides were the most effective acceptor substrates analyzed. The enzyme has a pH optimum between 6.5 and 7.0 and its activity is stimulated by Mn 21 and Co 21 ions. The apparent K m and V max values of the arabinofuranosyltransferase for UDP-arabinofuranose are 243 mM and 243 pmol min 21 mg protein 21 , respectively. The highest enzyme activity was detected in the elongating regions of mung bean hypocotyls. The data show that UDP-arabinofuranose is the donor molecule for the generation of arabino-oligosaccharides composed of Araf residues.

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Section: Characterization Of Enzymatically Formed 2ab-labeled Arabinomentioning

confidence: 56%

Identification of a Mung Bean Arabinofuranosyltransferase That Transfers Arabinofuranosyl Residues onto (1, 5)-Linked α-l-Arabino-Oligosaccharides

et al. 2006

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“…More recently, ␤-1,4-GalT activity in mung bean detergent-treated microsomal membranes was identified that transferred up to eight galactosyl residues in a ␤-1,4-linkage onto the non-reducing end fluorescently labeled exogenous (1→4)-␤-galactooligosaccharide acceptors (386,387). Of the galactooligosaccharide acceptors used, i.e., degree of polymerization (DP) of 3-7, the galactoheptaose was a most effective acceptor although acceptors of DP 4-6 also functioned.…”

Section: Rg-i:galactosyltransferase (Rg-i:galt)mentioning

confidence: 99%

Cell Wall Polysaccharide Synthesis

Mohnen

Bar‐Peled

Somerville

2008

Biomass Recalcitrance

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Enzymic transfer of α-L-arabinopyranosyl residues to exogenous 1,4-linked β-D-galacto-oligosaccharides using solubilized mung bean (Vigna radiata) hypocotyl microsomes and UDP-β-L-arabinopyranose

Ishii

Ono

Ohnishi‐Kameyama

et al. 2005

Planta

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A single alpha-L-arabinopyranosyl (alpha-L-Arap) residue was shown, by a combination of chemical and spectroscopic methods, to be transferred to O-4 of the nonreducing terminal galactosyl (Gal) residue of 2-aminobenzamide (2AB)-labeled galacto-oligosaccharides when these oligosaccharides were reacted with UDP-ss-L-arabinopyranose (UDP-ss-L-Arap) in the presence of a Triton X-100-soluble extract of microsomal membranes isolated from mung bean (Vigna radiata, L. Wilezek) hypocotyls. Maximum-(1-->4)-arabinopyranosyltransferase activity was obtained at pH 6.0-6.5 and 20 degrees C in the presence of 25 mM Mn2+. The enzyme had an apparent K m of 45 microM for the 2AB-labeled galactoheptasaccharide and 330 microM for UDP-ss-L-Arap. A series of 2AB-labeled galacto-oligosaccharides with a degree of polymerization (DP) between 6 and 10 that contained a single alpha-L-Arap residue linked to the former nonreducing terminal Gal residue were generated when the 2AB-labeled galactohexasaccharide (Gal6-2AB) was reacted with UDP- ss-L-Ara p in the presence of UDP-beta-D-Galp and the solubilized microsomal fraction. The mono-arabinosylated galacto-oligosaccharides are not acceptor substrates for the galactosyltransferase activities known to be present in mung bean microsomes. These results show that mung bean hypocotyl microsomes contain an enzyme that catalyzes the transfer of Arap to the nonreducing Gal residue of galacto-oligosaccharides and suggest that the presence of a alpha-L-Arap residue on the former terminal Gal residue prevents galactosylation of galacto-oligosaccharides.

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Assignment of the 1H and 13C NMR spectra of 2-aminobenzamide-labeled galacto- and arabinooligosaccharides

Cited by 6 publications

References 11 publications

Identification of a Mung Bean Arabinofuranosyltransferase That Transfers Arabinofuranosyl Residues onto (1, 5)-Linked α-l-Arabino-Oligosaccharides

Identification of a Mung Bean Arabinofuranosyltransferase That Transfers Arabinofuranosyl Residues onto (1, 5)-Linked α-l-Arabino-Oligosaccharides

Cell Wall Polysaccharide Synthesis

Enzymic transfer of α-L-arabinopyranosyl residues to exogenous 1,4-linked β-D-galacto-oligosaccharides using solubilized mung bean (Vigna radiata) hypocotyl microsomes and UDP-β-L-arabinopyranose

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