Article
Functional dissection of the N-terminal sequence of Clostridium sp. G0005 glucoamylase: identification of components critical for folding the catalytic domain and for constructing the active site structure.
Applied microbiology and biotechnology - 1 Mar 2017
Sakaguchi Masayoshi, Matsushima Yudai, Nagamine Yusuke, Matsuhashi Tomoki, Honda Shotaro, Okuda Shoi, Ohno Misa, Sugahara Yasusato, Shin Yongchol, Oyama Fumitaka, Kawakita Masao
Abstract excerpt
Clostridium sp. G0005 glucoamylase (CGA) is composed of a β-sandwich domain (BD), a linker, and a catalytic domain (CD). In the present study, CGA was expressed in Escherichia coli as inclusion bodies when the N-terminal region (39 amino acid residues) of the BD was truncated. To further elucidate the role of the N-terminal region of the BD, we constructed N-terminally truncated proteins (Δ19, Δ24, Δ29, and Δ34)...
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