Nitrile hydratase (NHase), an excellent bio‐catalyst for the synthesis of amide compounds, was composed of two heterologous subunits. A thermoalkaliphilic NHase NHCTA1 (Tm = 71.3°C) obtained by in silico screening in our study exhibited high flex...
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https://www.riss.kr/link?id=O111626943
2021년
-
0887-3585
1097-0134
SCI;SCIE;SCOPUS
학술저널
978-987 [※수록면이 p5 이하이면, Review, Columns, Editor's Note, Abstract 등일 경우가 있습니다.]
0
상세조회0
다운로드다국어 초록 (Multilingual Abstract)
Nitrile hydratase (NHase), an excellent bio‐catalyst for the synthesis of amide compounds, was composed of two heterologous subunits. A thermoalkaliphilic NHase NHCTA1 (Tm = 71.3°C) obtained by in silico screening in our study exhibited high flex...
Nitrile hydratase (NHase), an excellent bio‐catalyst for the synthesis of amide compounds, was composed of two heterologous subunits. A thermoalkaliphilic NHase NHCTA1 (Tm = 71.3°C) obtained by in silico screening in our study exhibited high flexibility of α‐subunit but excellent thermostability, as opposed to previous examples. To gain a deeper structural insight into the thermostability of NHCTA1, comparative molecular dynamics simulation of NHCTA1 and reported NHases was carried out. By comparison, we speculated that β‐subunit played a key role in adjusting the flexibility of α‐subunit and the different conformations of linker in “α5‐helix‐coil ring” supersecondary structure of β‐subunit can affect the interaction between β‐subunit and α‐subunit. Mutant NHCTA1‐α6C with a random coil linker and mutant NHCTA1‐αβγ with a truncated linker were therefore constructed to understand the impact on NHCTA1 thermostability by varying the supersecondary structure. The varied thermostability of NHCTA1‐α6C and NHCTA1‐αβγ (Tmα6C = 74.4°C, Tmαβγ = 65.6°C) verified that the flexibility of α‐subunit adjusted by β‐subunit was relevant to the stability of NHCTA1. This study gained an insight into the NNHCTA1 thermostability by virtual dynamics comparison and experimental studies without crystallization, and this approach could be applied to other industrial‐important enzymes.
Cover Image, Volume 89, Issue 8
Mask blast with a new chemical logic of amino acids for improved protein function prediction