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• W2313959970 abstract "The active site for the family GH38 class II α-mannosidase is constituted in part by a divalent metal ion, mostly Zn2+, as revealed in the crystal structures of enzymes from both animal and bacterial sources. The metal ion coordinates to the bound substrate and side chains of conserved amino acid residues. Recently, evidence has accumulated that class II α-mannosidase is active in complex with a range of divalent metal ions. In the present work, with employment of the class II α-mannosidase, ManA, from the hyperthermophilic archaeon Sulfolobus solfataricus, we explored the influence of the divalent metal ion on the associated steady-state kinetic parameters, KM and kcat, for various substrates. With p-nitrophenyl-α-d-mannoside as a substrate, the enzyme showed activity in the presence of Co2+, Cd2+, Mn2+, and Zn2+, whereas Ni2+ and Cu2+ were inhibitory and nonactivating. Co2+ was the preferred metal ion, with a kcat/KM value of about 120 mM–1 s–1, 6 times higher than that with Cd2+ and Zn2+ and 10 times higher than that with Mn2+. With α-1,2-, α-1,3-, α-1,4-, or α-1,6-mannobiose as a substrate, Co2+ was the only metal ion promoting hydrolysis of all substrates; however, Mn2+, Cd2+, and Zn2+ could substitute to a varying extent. A change in the divalent metal ion generally affected the KM for the hydrolysis of p-nitrophenyl-α-d-mannoside; however, changes in both kcat and KM for the hydrolysis of α-mannobioses were observed, along with changing preferences for the glycosidic linkage. Finally, it was found that the metal ion and substrate bind in that order via a steady-state, ordered, sequential mechanism." @default.
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• W2313959970 date "2012-09-28" @default.
• W2313959970 modified "2023-09-27" @default.
• W2313959970 title "Metal-Ion Dependent Catalytic Properties of <i>Sulfolobus solfataricus</i> Class II α-Mannosidase" @default.
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• W2313959970 doi "https://doi.org/10.1021/bi301096a" @default.
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