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- W2663310607 abstract "Thermostable α-amylases have many industrial applications and are therefore continuously explored from novel sources. We present the characterization of a novel putative α-amylase gene product (Tp-AmyS) cloned from Thermotoga petrophila. The purified recombinant enzyme is highly thermostable and able to hydrolyze starch into dextrin between 90 and 100 °C, with optimum activity at 98 °C and pH 8.5. The activity increased in the presence of Rb1 +, K1 + and Ca2 + ions, whereas other ions inhibited activity. The crystal structure of Tp-AmyS at 1.7 Å resolution showed common features of the GH-13 family, however was apparently found to be a dimer. Several residues from one monomer interacted with a docked acarbose, an inhibitor of Tp-AmyS, in the other monomer, suggesting catalytic cooperativity within the dimer. The most striking feature of the dimer was that it resembled the dimerization of salivary amylase from a previous crystal structure, and thus could be a functional feature of some amylases." @default.
- W2663310607 created "2017-06-30" @default.
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- W2663310607 date "2017-10-01" @default.
- W2663310607 modified "2023-09-26" @default.
- W2663310607 title "Functional characterization and crystal structure of thermostable amylase from Thermotoga petrophila , reveals high thermostability and an unusual form of dimerization" @default.
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- W2663310607 doi "https://doi.org/10.1016/j.bbapap.2017.06.015" @default.
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