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Tunnel Engineering for Modulating The Substrate Preference in Decarbonylase P450BsβHI
release_npuiiewasbcg3chgdv5t2bbhte
by
Shuaiqi Meng,
Ruipeng An,
Zhongyu Li,
Ulrich Schwaneberg,
Yu Ji,
Mehdi D. Davari,
Wang Fang,
Meng Wang,
Meng Qin,
Kaili Nie,
Luo Liu
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by Research Square.
2020
Abstract
<jats:title>Abstract</jats:title>
An active site normally locates inside of enzymes, substrates should go through the tunnel to access the active site. Tunnel engineering is a powerful strategy for refining the catalytic properties of enzymes. Here, P450<jats:sub>Bsβ</jats:sub>HI (Q85H/ V170I) derived from hydroxylase P450<jats:sub>Bsβ</jats:sub> from <jats:italic>Bacillus subtilis</jats:italic> was chosen as study model, which is reported as a potential decarbonylase. However, this enzyme showed low decarboxylase activity towards long-chain fatty acids. Here, a tunnel engineering campaign was performed for modulating the substrate preference and improving the decarbonylase activity of P450<jats:sub>Bsβ</jats:sub>HI. The finally obtained BsβHI-F79A variant had a 15.2-fold improved conversion for palmitic acid; BsβHI-F173V variant had a 3.9-fold improved conversion for pentadecanoic acid. The study demonstrates how the substrate preference can be modulated by tunnel engineering strategy.
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