Differential active site loop conformations mediate promiscuous activities in the lactonase SsoPox.
Enzymes are proficient catalysts that enable fast rates of Michaelis-complex formation, the chemical step and products release. These different steps may require different conformational states of the active site that have distinct binding properties. Moreover, the conformational flexibility of the...
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| Auteurs principaux: | , , , |
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| Format: | article |
| Langue: | EN |
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Public Library of Science (PLoS)
2013
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| Accès en ligne: | https://doaj.org/article/076e310a0a9341e4b1de414da4202dfe |
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