Structural highlights
Function
[4OT1_PSEPU] Catalyzes the ketonization of 2-hydroxymuconate stereoselectively to yield 2-oxo-3-hexenedioate.[1]
Publication Abstract from PubMed
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.
Substituting the catalytic proline of 4-oxalocrotonate tautomerase with non-canonical analogues reveals a finely tuned catalytic system.,Lukesch MS, Pavkov-Keller T, Gruber K, Zangger K, Wiltschi B Sci Rep. 2019 Feb 25;9(1):2697. doi: 10.1038/s41598-019-39484-9. PMID:30804446[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Chen LH, Kenyon GL, Curtin F, Harayama S, Bembenek ME, Hajipour G, Whitman CP. 4-Oxalocrotonate tautomerase, an enzyme composed of 62 amino acid residues per monomer. J Biol Chem. 1992 Sep 5;267(25):17716-21. PMID:1339435
- ↑ Lukesch MS, Pavkov-Keller T, Gruber K, Zangger K, Wiltschi B. Substituting the catalytic proline of 4-oxalocrotonate tautomerase with non-canonical analogues reveals a finely tuned catalytic system. Sci Rep. 2019 Feb 25;9(1):2697. doi: 10.1038/s41598-019-39484-9. PMID:30804446 doi:http://dx.doi.org/10.1038/s41598-019-39484-9
