A Novel highly thermostable branched-chain amino acid aminotransferase from the crenarchaeon Vulcanisaeta moutnovskia
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- 作者：Tatiana N. Stekhanovaa ; tstekh@yandex.ru" class="auth_mail" title="E-mail the corresponding author ; Andrey L. Rakitinb ; Andrey V. Mardanovb ; Ekaterina Yu. Bezsudnovaa ; Vladimir O. Popova ; c
- 关键词：BCAA ; branched-chain amino acid ; BCAT ; branched-chain amino acid aminotransferase ; PLP ; pyridoxal 5&prime ; -phosphate ; PMP ; pyridoxamine 5&prime ; -phosphate ; (R)-MBA ; (R)-α-methylbenzylamine ; AlaDH ; alanine dehydrogenase ; LDH ; lactate dehydrogenase
- 刊名：Enzyme and Microbial Technology
- 出版年：2017
- 出版时间：January 2017
- 年：2017
- 卷：96
- 期：Complete
- 页码：127-134
- 全文大小：865 K
文摘
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A novel archaeal BCAT was expressed in E. coli, purified and characterized.
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Enzyme showed a broad spectrum and unique combination of substrate specificities.
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VMUT0738 showed high (S)-enantioselectivity, thermostability, resistance to solvents.
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Two sequence motifs characteristic of BCATs from Thermoproteaceae were revealed.