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Bioresour. Technol., Dec 27 2023, 394 S0960-8524(23)01676-0 | https://doi.org/10.1016/j.biortech.2023.130248
Tunnel engineering of gas-converting enzymes for inhibitor retardation and substrate acceleration
Suk Min Kim a, Sung Heuck Kang a, Byoung Wook Jeon a, Yong Hwan Kim a,b
aSchool of Energy and Chemical Engineering, Ulsan National Institute of Science and Technology (UNIST), 50 UNIST-gil, Ulsan 44919, Republic of Korea
bGraduate School of Carbon Neutrality, Ulsan National Institute of Science and Technology (UNIST), 50 UNIST-gil, Ulsan 44919, Republic of Korea
Corresponding authors : Suk Min Kim, Yong Hwan Kim
Abstract
Carbon monoxide dehydrogenase (CODH), formate dehydrogenase (FDH), hydrogenase (H2ase), and nitrogenase (N2ase) are crucial enzymatic catalysts that facilitate the conversion of industrially significant gases such as CO, CO
2, H
2, and N
2. The tunnels in the gas-converting enzymes serve as conduits for these low molecular weight gases to access deeply buried catalytic sites. The identification of the substrate tunnels is imperative for comprehending the substrate selectivity mechanism underlying these gas-converting enzymes. This knowledge also holds substantial value for industrial applications, particularly in addressing the challenges associated with separation and utilization of byproduct gases. In this comprehensive review, we delve into the emerging field of tunnel engineering, presenting a range of approaches and analyses. Additionally, we propose methodologies for the systematic design of enzymes, with the ultimate goal of advancing protein engineering strategies.
논문정보
- Review Paper
- 2023년 12월 (BRIC 등록일 2024-01-08)
- 국내 연구진
- 생명과학 > 생물공학
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