| Autor: |
Chun-Liang Chen, Lake N. Paul, James C. Mermoud, Calvin Nicklaus Steussy, Cynthia V. Stauffacher |
| Jazyk: |
angličtina |
| Rok vydání: |
2020 |
| Předmět: |
|
| Zdroj: |
Nature Communications, Vol 11, Iss 1, Pp 1-13 (2020) |
| Druh dokumentu: |
article |
| ISSN: |
2041-1723 |
| DOI: |
10.1038/s41467-020-17733-0 |
| Popis: |
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. |
| Databáze: |
Directory of Open Access Journals |
| Externí odkaz: |
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