Visualizing the enzyme mechanism of mevalonate diphosphate decarboxylase
Mevalonate diphosphate decarboxylase (MDD) is a key enzyme in the mevalonate pathway and catalyses the decarboxylation of mevalonate-5-diphosphate to isopentenyl diphosphate. Here, the authors provide insights into the conformational changes that occur during substrate binding of MDD and the subsequ...
| Main Authors: | , , , , |
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| Format: | Article |
| Language: | English |
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Nature Portfolio
2020-08-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-020-17733-0 |
| _version_ | 1819126501202722816 |
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| author | Chun-Liang Chen Lake N. Paul James C. Mermoud Calvin Nicklaus Steussy Cynthia V. Stauffacher |
| author_facet | Chun-Liang Chen Lake N. Paul James C. Mermoud Calvin Nicklaus Steussy Cynthia V. Stauffacher |
| author_sort | Chun-Liang Chen |
| collection | DOAJ |
| description | Mevalonate diphosphate decarboxylase (MDD) is a key enzyme in the mevalonate pathway and catalyses the decarboxylation of mevalonate-5-diphosphate to isopentenyl diphosphate. Here, the authors provide insights into the conformational changes that occur during substrate binding of MDD and the subsequent enzymatic reaction steps by determining the substrate and intermediate bound crystal structures of Enterococcus faecalis MDD. |
| first_indexed | 2024-12-22T07:57:02Z |
| format | Article |
| id | doaj.art-b0d17fe2854d4bb9a893293053f08b6e |
| institution | Directory Open Access Journal |
| issn | 2041-1723 |
| language | English |
| last_indexed | 2024-12-22T07:57:02Z |
| publishDate | 2020-08-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Nature Communications |
| spelling | doaj.art-b0d17fe2854d4bb9a893293053f08b6e2022-12-21T18:33:20ZengNature PortfolioNature Communications2041-17232020-08-0111111310.1038/s41467-020-17733-0Visualizing the enzyme mechanism of mevalonate diphosphate decarboxylaseChun-Liang Chen0Lake N. Paul1James C. Mermoud2Calvin Nicklaus Steussy3Cynthia V. Stauffacher4Department of Biological Sciences, Purdue UniversityBioAnalysis, LLCDepartment of Biological Sciences, Purdue UniversityDepartment of Biological Sciences, Purdue UniversityDepartment of Biological Sciences, Purdue UniversityMevalonate diphosphate decarboxylase (MDD) is a key enzyme in the mevalonate pathway and catalyses the decarboxylation of mevalonate-5-diphosphate to isopentenyl diphosphate. Here, the authors provide insights into the conformational changes that occur during substrate binding of MDD and the subsequent enzymatic reaction steps by determining the substrate and intermediate bound crystal structures of Enterococcus faecalis MDD.https://doi.org/10.1038/s41467-020-17733-0 |
| spellingShingle | Chun-Liang Chen Lake N. Paul James C. Mermoud Calvin Nicklaus Steussy Cynthia V. Stauffacher Visualizing the enzyme mechanism of mevalonate diphosphate decarboxylase Nature Communications |
| title | Visualizing the enzyme mechanism of mevalonate diphosphate decarboxylase |
| title_full | Visualizing the enzyme mechanism of mevalonate diphosphate decarboxylase |
| title_fullStr | Visualizing the enzyme mechanism of mevalonate diphosphate decarboxylase |
| title_full_unstemmed | Visualizing the enzyme mechanism of mevalonate diphosphate decarboxylase |
| title_short | Visualizing the enzyme mechanism of mevalonate diphosphate decarboxylase |
| title_sort | visualizing the enzyme mechanism of mevalonate diphosphate decarboxylase |
| url | https://doi.org/10.1038/s41467-020-17733-0 |
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