| Title : Structural and functional insights into the enzymatic activities of lipases from Burkholderia stagnalis and Burkholderia plantarii - Kataoka_2024_FEBS.Lett__ |
| Author(s) : Kataoka S , Kawamoto S , Kitagawa S , Kugimiya W , Tsumura K , Akutsu Y , Kubota T , Ishikawa K |
| Ref : FEBS Letters , : , 2024 |
| Abstract : Lipases with high interesterification activity are important enzymes for industrial use. The lipase from Burkholderiastagnalis (BsL) exhibits higher interesterification activity than that from Burkholderiaplantarii (BpL) despite their significant sequence similarity. In this study, we determined the crystal structure of BsL at 1.40A resolution. Utilizing structural insights, we have successfully augmented the interesterification activity of BpL by over twofold. This enhancement was achieved by substituting threonine with serine at position 289 through forming an expansive space in the substrate-binding site. Additionally, we discuss the activity mechanism based on the kinetic parameters. Our study sheds light on the structural determinants of the interesterification activity of lipase. |
| ESTHER : Kataoka_2024_FEBS.Lett__ |
| PubMedSearch : Kataoka_2024_FEBS.Lett__ |
| PubMedID: 38658173 |
| Gene_locus related to this paper: 9burk-a0a108c1v7 |
| Gene_locus related to this paper: 9burk-a0a108c1v7 |
Kataoka S, Kawamoto S, Kitagawa S, Kugimiya W, Tsumura K, Akutsu Y, Kubota T, Ishikawa K (2024)
Structural and functional insights into the enzymatic activities of lipases from Burkholderia stagnalis and Burkholderia plantarii
FEBS Letters
:
Kataoka S, Kawamoto S, Kitagawa S, Kugimiya W, Tsumura K, Akutsu Y, Kubota T, Ishikawa K (2024)
FEBS Letters
: