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Synthetic Potential of Molluscan Sulfatases for the Library Synthesis of Regioselectively O-Sulfonated D-Galacto-Sugars

Authors

  • Hirotaka Uzawa Dr.,

    1. Laboratory of Advanced Bioelectronics National Institute of Advanced Industrial Science and Technology (AIST) Central 5, 11-1 Higashi, Tsukuba 305 – 8565, Japan, Fax: (+81) 29861-4680
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  • Yoshihiro Nishida Prof. Dr.,

    1. Department of Molecular Design and Engineering Graduate School of Engineering, Nagoya University Chikusa, Nagoya 464-8603, Japan
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  • Kenji Sasaki,

    1. Department of Molecular Design and Engineering Graduate School of Engineering, Nagoya University Chikusa, Nagoya 464-8603, Japan
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  • Norihiko Minoura Dr.,

    1. Laboratory of Advanced Bioelectronics National Institute of Advanced Industrial Science and Technology (AIST) Central 5, 11-1 Higashi, Tsukuba 305 – 8565, Japan, Fax: (+81) 29861-4680
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  • Kazukiyo Kobayashi Prof. Dr.

    1. Department of Molecular Design and Engineering Graduate School of Engineering, Nagoya University Chikusa, Nagoya 464-8603, Japan
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Abstract

The substrate specificities of three molluscan sulfatases (E.C. 3.1.6.1; snail, abalone, and limpet origins) were investigated with assorted p-nitrophenyl (pNP) di-O-sulfonated β-D-galactopyranosides and β-lactosides [3,6-SO3Gal (1), 3′,6′-SO3Lac (2), 4, 6SO3Gal (3), 2,6-SO3Gal (4), 3,4-SO3Gal (5), and 3,6-SO3GalNAc (6); Ac, acetyl; Gal, galactose; Lac, lactose] together with mono-O-sulfonated β-D-galactopyranoside [pNP 3SO3-Gal (7)] and tri-O-sulfonated α-D-galactopyranoside [2,3,6-SO3-α-Gal (11)]. Some notable differences between the substrate specificity of the three sulfatases were disclosed; snail sulfatase hydrolyzed the 3O- and 2O-sulfo groups of 1 and 4, respectively, to afford 6SO3Gal (9) in high yields, while the abalone enzyme did not act on 4. Only the limpet enzyme could cleave the 3O-sulfo groups of 7 to give pNP β-galactoside. In contrast, every enzyme could utilize 11 as a good substrate to afford a mixture of 6SO3-α-Gal (13) and 2,6-SO3α-Gal (12). None of the enzymes could cleave the O-sulfo groups of 5 and 6, which indicates that a primary 6O-sulfo group tends to promote the enzymatic hydrolysis of O-sulfo groups at the secondary positions.

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