Self-transferring Product Inhibition Observed during the Hydrolysis of Aryl-β-D-Glucopyranosides by a β-Glucosidase from Agrobacterium tumefaciens

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  • Kitaoka Motomitsu
    Enzyme Laboratory, National Food Research Institute, National Agriculture and Food Research Organization
  • Takahashi Tomoya
    Enzyme Laboratory, National Food Research Institute, National Agriculture and Food Research Organization
  • Ying Li
    Enzyme Laboratory, National Food Research Institute, National Agriculture and Food Research Organization State Key Laboratories for Agro-biotechnology and College of Biological Sciences, China Agricultural University
  • Hayashi Kiyoshi
    Enzyme Laboratory, National Food Research Institute, National Agriculture and Food Research Organization

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  • Self-transferring Product Inhibition Observed during the Hydrolysis of Aryl-.BETA.-D-Glucopyranosides by a .BETA.-Glucosidase from Agrobacterium tumefaciens

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The time profile of an enzymatic reaction at an early stage is generally considered to be linear. We observed that the time profile of the hydrolysis of 1 mM p-nitrophenyl-β-D-glucoside (pNP-Glc) by a β-glucosidase obtained from Agrobacterium tumefaciens (Cbg1) was not linear before 5% of the substrate was consumed, even though the initial concentration of the substrate was much higher than its Km value. The time profiles obtained with higher concentrations of pNP-Glc suggested that the time profile was the function of the absolute concentration of p-nitrophenol (pNP). The addition of various alcohols made the time profile linear. A self-transferring product inhibition model was constructed in which the pNP generated during the hydrolysis acts as an acceptor substrate to inhibit the hydrolysis. The theoretical curve agreed well with the experimental data.

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