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Substituting the catalytic proline of 4-oxalocrotonate tautomerase with non-canonical analogues reveals a finely tuned catalytic system
The enzyme 4-oxalocrotonate tautomerase shows remarkable catalytic versatility due to the secondary amine of its N-terminal proline moiety. In this work, we incorporated a range of proline analogues into the enzyme and examined the effects on structure and activity. While the structure of the enzyme...
Autores principales: | Lukesch, Michael S., Pavkov-Keller, Tea, Gruber, Karl, Zangger, Klaus, Wiltschi, Birgit |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6389900/ https://www.ncbi.nlm.nih.gov/pubmed/30804446 http://dx.doi.org/10.1038/s41598-019-39484-9 |
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