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麦角硫因合成中关键酶的催化机制

The Catalytic Mechanism of Key Enzymes Involved in the Synthesis of Ergothioneine in .

作者信息

Li Zheng, Ding Jianjun, Huang Wen, Bian Yinbing, Feng Xi, Liu Ying

机构信息

College of Food Science & Technology, Huazhong Agricultural University, Wuhan 430070, China.

School of Food Science and Technology, Jiangnan University, Wuxi 214122, China.

出版信息

Molecules. 2024 Dec 20;29(24):6005. doi: 10.3390/molecules29246005.

DOI:10.3390/molecules29246005
PMID:39770093
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC11677154/
Abstract

C-S lyase is a crucial enzyme responsible for the formation of sulfur-containing flavor compounds in . We investigated the involvement of C-S lyase in the synthesis of ergothioneine (EGT) in , a high-producing edible mushroom. Through experimental and computational approaches, we identified 2, a C-S lyase, as a key enzyme involved in EGT synthesis in . We characterized the enzymatic catalytic mechanism of Egt1 and Egt2, the two enzymes primarily catalyzing EGT synthesis in fungi. The results showed that Egt1 interacted with His, SAM, and Cys to form the intermediate product Her-sul, while Egt2, a PLP-dependent enzyme, cleaved the C-S bond on Her-sul to produce EGT. However, our findings suggested that Egt2 in might not form a covalent bond with PLP, unlike the previously reported catalytic mechanism of Egt2 involving covalent catalysis. The study provided new insights into the synthesis pathway of EGT in and highlighted the need for further investigation into the catalytic mechanism of Egt2 in this species.

摘要

C-S裂解酶是一种关键酶,负责在……中形成含硫风味化合物。我们研究了C-S裂解酶在高产食用菌……中麦角硫因(EGT)合成中的作用。通过实验和计算方法,我们确定了C-S裂解酶2是参与……中EGT合成的关键酶。我们表征了Egt1和Egt2这两种主要催化真菌中EGT合成的酶的催化机制。结果表明,Egt1与组氨酸、SAM和半胱氨酸相互作用形成中间产物Her-sul,而Egt2是一种依赖PLP的酶,它裂解Her-sul上的C-S键以产生EGT。然而,我们的研究结果表明,与之前报道的涉及共价催化的Egt2催化机制不同,……中的Egt2可能不会与PLP形成共价键。该研究为……中EGT的合成途径提供了新的见解,并强调了进一步研究该物种中Egt2催化机制的必要性。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e51a/11677154/286df8232bb9/molecules-29-06005-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e51a/11677154/d7919ae68b51/molecules-29-06005-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e51a/11677154/35a712e3a631/molecules-29-06005-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e51a/11677154/b33b02b17303/molecules-29-06005-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e51a/11677154/6adb8da83453/molecules-29-06005-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e51a/11677154/9cc3f4285932/molecules-29-06005-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e51a/11677154/286df8232bb9/molecules-29-06005-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e51a/11677154/d7919ae68b51/molecules-29-06005-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e51a/11677154/35a712e3a631/molecules-29-06005-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e51a/11677154/b33b02b17303/molecules-29-06005-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e51a/11677154/6adb8da83453/molecules-29-06005-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e51a/11677154/9cc3f4285932/molecules-29-06005-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e51a/11677154/286df8232bb9/molecules-29-06005-g006.jpg

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Significant Improvement of Both Catalytic Efficiency and Stability of Fructosyltransferase from by Structure-Guided Engineering of Key Residues in the Conserved Sequence of the Catalytic Domain.通过对催化结构域保守序列中关键残基的结构指导工程改造,显著提高果糖基转移酶的催化效率和稳定性。
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