The Catalytic Mechanism of Key Enzymes Involved in the Synthesis of Ergothioneine in <i>Lentinula edodes</i>
C-S lyase is a crucial enzyme responsible for the formation of sulfur-containing flavor compounds in <i>Lentinula edodes</i>. We investigated the involvement of C-S lyase in the synthesis of ergothioneine (EGT) in <i>L. edodes</i>, a high-producing edible mushroom. Through ex...
Saved in:
| Main Authors: | , , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
MDPI AG
2024-12-01
|
| Series: | Molecules |
| Subjects: | |
| Online Access: | https://www.mdpi.com/1420-3049/29/24/6005 |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
| _version_ | 1850239524144152576 |
|---|---|
| author | Zheng Li Jianjun Ding Wen Huang Yinbing Bian Xi Feng Ying Liu |
| author_facet | Zheng Li Jianjun Ding Wen Huang Yinbing Bian Xi Feng Ying Liu |
| author_sort | Zheng Li |
| collection | DOAJ |
| description | C-S lyase is a crucial enzyme responsible for the formation of sulfur-containing flavor compounds in <i>Lentinula edodes</i>. We investigated the involvement of C-S lyase in the synthesis of ergothioneine (EGT) in <i>L. edodes</i>, a high-producing edible mushroom. Through experimental and computational approaches, we identified <i>Lecsl</i>2, a C-S lyase, as a key enzyme involved in EGT synthesis in <i>L. edodes</i>. 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 <i>L. edodes</i> 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 <i>L. edodes</i> and highlighted the need for further investigation into the catalytic mechanism of Egt2 in this species. |
| format | Article |
| id | doaj-art-3a6893d632494ce49f8f2ffb2dc145db |
| institution | OA Journals |
| issn | 1420-3049 |
| language | English |
| publishDate | 2024-12-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Molecules |
| spelling | doaj-art-3a6893d632494ce49f8f2ffb2dc145db2025-08-20T02:01:08ZengMDPI AGMolecules1420-30492024-12-012924600510.3390/molecules29246005The Catalytic Mechanism of Key Enzymes Involved in the Synthesis of Ergothioneine in <i>Lentinula edodes</i>Zheng Li0Jianjun Ding1Wen Huang2Yinbing Bian3Xi Feng4Ying Liu5College of Food Science & Technology, Huazhong Agricultural University, Wuhan 430070, ChinaSchool of Food Science and Technology, Jiangnan University, Wuxi 214122, ChinaCollege of Food Science & Technology, Huazhong Agricultural University, Wuhan 430070, ChinaInstitute of Applied Mycology, Huazhong Agricultural University, Wuhan 430070, ChinaDepartment of Nutrition, Food Science and Packaging, San Jose State University, San Jose, CA 95192, USACollege of Food Science & Technology, Huazhong Agricultural University, Wuhan 430070, ChinaC-S lyase is a crucial enzyme responsible for the formation of sulfur-containing flavor compounds in <i>Lentinula edodes</i>. We investigated the involvement of C-S lyase in the synthesis of ergothioneine (EGT) in <i>L. edodes</i>, a high-producing edible mushroom. Through experimental and computational approaches, we identified <i>Lecsl</i>2, a C-S lyase, as a key enzyme involved in EGT synthesis in <i>L. edodes</i>. 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 <i>L. edodes</i> 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 <i>L. edodes</i> and highlighted the need for further investigation into the catalytic mechanism of Egt2 in this species.https://www.mdpi.com/1420-3049/29/24/6005<i>Lentinula</i> <i>edodes</i>ergothioneineC-S lyasebiocatalysis |
| spellingShingle | Zheng Li Jianjun Ding Wen Huang Yinbing Bian Xi Feng Ying Liu The Catalytic Mechanism of Key Enzymes Involved in the Synthesis of Ergothioneine in <i>Lentinula edodes</i> Molecules <i>Lentinula</i> <i>edodes</i> ergothioneine C-S lyase biocatalysis |
| title | The Catalytic Mechanism of Key Enzymes Involved in the Synthesis of Ergothioneine in <i>Lentinula edodes</i> |
| title_full | The Catalytic Mechanism of Key Enzymes Involved in the Synthesis of Ergothioneine in <i>Lentinula edodes</i> |
| title_fullStr | The Catalytic Mechanism of Key Enzymes Involved in the Synthesis of Ergothioneine in <i>Lentinula edodes</i> |
| title_full_unstemmed | The Catalytic Mechanism of Key Enzymes Involved in the Synthesis of Ergothioneine in <i>Lentinula edodes</i> |
| title_short | The Catalytic Mechanism of Key Enzymes Involved in the Synthesis of Ergothioneine in <i>Lentinula edodes</i> |
| title_sort | catalytic mechanism of key enzymes involved in the synthesis of ergothioneine in i lentinula edodes i |
| topic | <i>Lentinula</i> <i>edodes</i> ergothioneine C-S lyase biocatalysis |
| url | https://www.mdpi.com/1420-3049/29/24/6005 |
| work_keys_str_mv | AT zhengli thecatalyticmechanismofkeyenzymesinvolvedinthesynthesisofergothioneineinilentinulaedodesi AT jianjunding thecatalyticmechanismofkeyenzymesinvolvedinthesynthesisofergothioneineinilentinulaedodesi AT wenhuang thecatalyticmechanismofkeyenzymesinvolvedinthesynthesisofergothioneineinilentinulaedodesi AT yinbingbian thecatalyticmechanismofkeyenzymesinvolvedinthesynthesisofergothioneineinilentinulaedodesi AT xifeng thecatalyticmechanismofkeyenzymesinvolvedinthesynthesisofergothioneineinilentinulaedodesi AT yingliu thecatalyticmechanismofkeyenzymesinvolvedinthesynthesisofergothioneineinilentinulaedodesi AT zhengli catalyticmechanismofkeyenzymesinvolvedinthesynthesisofergothioneineinilentinulaedodesi AT jianjunding catalyticmechanismofkeyenzymesinvolvedinthesynthesisofergothioneineinilentinulaedodesi AT wenhuang catalyticmechanismofkeyenzymesinvolvedinthesynthesisofergothioneineinilentinulaedodesi AT yinbingbian catalyticmechanismofkeyenzymesinvolvedinthesynthesisofergothioneineinilentinulaedodesi AT xifeng catalyticmechanismofkeyenzymesinvolvedinthesynthesisofergothioneineinilentinulaedodesi AT yingliu catalyticmechanismofkeyenzymesinvolvedinthesynthesisofergothioneineinilentinulaedodesi |