A Novel highly thermostable branched-chain amino acid aminotransferase from the crenarchaeon Vulcanisaeta moutnovskia
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<p id="par0005">A novel archaeal BCAT was expressed in E. coli, purified and characterized.p>
<p id="par0010">Enzyme showed a broad spectrum and unique combination of substrate specificities.p>
<p id="par0015">VMUT0738 showed high (S)-enantioselectivity, thermostability, resistance to solvents.p>
<p id="par0020">Two sequence motifs characteristic of BCATs from Thermoproteaceae were revealed.p>

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