Cytochrome P450 Enzyme Design by Constraining the Catalytic Pocket in a Diffusion Model

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成果类型：

期刊论文

作者：

Wang, Qian;Liu, Xiaonan;Zhang, Hejian;Chu, Huanyu;Shi, Chao;...

通讯作者：

Cheng, Jian;Jiang, HF;Chang, ZZ

作者机构：

[Huang, Rong; Jiang, Huifeng; Li, Jing; Liu, Tian; Zhang, Lei; Liu, Pi; Liu, Yuwan; Liu, Xiaonan; Cheng, Jian; Chu, Huanyu; Zhu, Xiaoxi; Chang, Hong; Wang, Qian; Jiang, HF; Zhang, Hejian; Bai, Jie] Chinese Acad Sci, Tianjin Inst Ind Biotechnol, Key Lab Engn Biol Low Carbon Mfg, Tianjin 300308, Peoples R China.

[Liu, Xiaonan; Chu, Huanyu; Zhu, Xiaoxi; Wang, Qian] Univ Chinese Acad Sci, Beijing 100049, Peoples R China.

[Huang, Rong; Jiang, Huifeng; Li, Jing; Liu, Tian; Liu, Pi; Liu, Yuwan; Liu, Xiaonan; Cheng, Jian; Zhu, Xiaoxi; Chang, Hong; Wang, Qian; Jiang, HF; Zhang, Hejian; Bai, Jie] Natl Ctr Technol Innovat Synthet Biol, Tianjin 300308, Peoples R China.

[Zhang, Hejian] Tianjin Univ Sci & Technol, Coll Biotechnol, Tianjin 300457, Peoples R China.

[Shi, Chao; Chang, Zhenzhan; Chen, Zhangxin] Peking Univ, Sch Basic Med Sci, Dept Biochem & Biophys, Beijing 100191, Peoples R China.

通讯机构：

[Cheng, J; Jiang, HF ] C

[Chang, ZZ ] P

Chinese Acad Sci, Tianjin Inst Ind Biotechnol, Key Lab Engn Biol Low Carbon Mfg, Tianjin 300308, Peoples R China.

Natl Ctr Technol Innovat Synthet Biol, Tianjin 300308, Peoples R China.

Peking Univ, Sch Basic Med Sci, Dept Biochem & Biophys, Beijing 100191, Peoples R China.

语种：

英文

期刊：

研究(英文)

ISSN：

2096-5168

年：

2024

卷：

页码：

0413

DOI：

10.34133/research.0413

基金类别：

National Key R&D Program of China [2019YFA0905700, 2021YFC2103500]; National Natural Science Foundation of China [32371499]; China Postdoctoral Science Foundation [2019M661032]; National Natural Science Foundation of China (NSFC) [31901026, 32171418]; Tianjin Synthetic Biotechnology Innovation Capacity Improvement Project [TSBICIPKJGG00202, TSBICIPCXRC015]; Tianjin Science Fund for Distinguished Young Scholars [18JCJQJC48300]

机构署名：

本校为其他机构

院系归属：

生命科学与技术学院

摘要：

Although cytochrome P450 enzymes are the most versatile biocatalysts in nature, there is insufficient comprehension of the molecular mechanism underlying their functional innovation process. Here, by combining ancestral sequence reconstruction, reverse mutation assay, and progressive forward accumulation, we identified 5 founder residues in the catalytic pocket of flavone 6-hydroxylase (F6H) and proposed a "3-point fixation" model to elucidate the functional innovation mechanisms of P450s in nature. According to this design principle of catalytic pocket, we further developed a de novo diffusio...

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Cytochrome P450 Enzyme Design by Constraining the Catalytic Pocket in a Diffusion Model

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