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

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

*Korrespondierende/r Autor/in für diese Arbeit

Publikation: Beitrag in einer FachzeitschriftArtikel

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.

Originalspracheenglisch
Aufsatznummer2697
FachzeitschriftScientific Reports
Jahrgang9
Ausgabenummer1
DOIs
PublikationsstatusVeröffentlicht - 1 Dez 2019

ASJC Scopus subject areas

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