Substituting the catalytic proline of 4-oxalocrotonate tautomerase with non-canonical analogues reveals a finely tuned catalytic system View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2019-12

AUTHORS

Michael S. Lukesch, Tea Pavkov-Keller, Karl Gruber, Klaus Zangger, Birgit Wiltschi

ABSTRACT

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 remained unperturbed, its promiscuous Michael-type activity was severely affected. This finding demonstrates how atomic changes in a biocatalytic system can abolish its activity. Our work provides a toolbox for successful generation of enzyme variants with non-canonical catalytic proline analogues. More... »

PAGES

2697

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/s41598-019-39484-9

DOI

http://dx.doi.org/10.1038/s41598-019-39484-9

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1112366334

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/30804446


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