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Structural and functional insights into the enzymatic activities of lipases from Burkholderia stagnalis and Burkholderia plantarii.
Kataoka, Saori; Kawamoto, Sayuri; Kitagawa, Sayuri; Kugimiya, Wataru; Tsumura, Kazunobu; Akutsu, Yukie; Kubota, Tomomi; Ishikawa, Kazuhiko.
Afiliación
  • Kataoka S; Research Institute for Creating the Future, Fuji Oil Holdings Inc., Tsukubamirai-shi, Japan.
  • Kawamoto S; Research Institute for Creating the Future, Fuji Oil Holdings Inc., Tsukubamirai-shi, Japan.
  • Kitagawa S; Research Institute for Creating the Future, Fuji Oil Holdings Inc., Tsukubamirai-shi, Japan.
  • Kugimiya W; Research Institute for Creating the Future, Fuji Oil Holdings Inc., Tsukubamirai-shi, Japan.
  • Tsumura K; Research Institute for Creating the Future, Fuji Oil Holdings Inc., Tsukubamirai-shi, Japan.
  • Akutsu Y; Biomedical Research Institute, National Institute of Advanced Industrial Science and Technology (AIST), Tsukuba, Japan.
  • Kubota T; Biomedical Research Institute, National Institute of Advanced Industrial Science and Technology (AIST), Tsukuba, Japan.
  • Ishikawa K; Biomedical Research Institute, National Institute of Advanced Industrial Science and Technology (AIST), Tsukuba, Japan.
FEBS Lett ; 598(11): 1411-1421, 2024 Jun.
Article en En | MEDLINE | ID: mdl-38658173
ABSTRACT
Lipases with high interesterification activity are important enzymes for industrial use. The lipase from Burkholderia stagnalis (BsL) exhibits higher interesterification activity than that from Burkholderia plantarii (BpL) despite their significant sequence similarity. In this study, we determined the crystal structure of BsL at 1.40 Å 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.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Burkholderia / Lipasa Idioma: En Revista: FEBS Lett Año: 2024 Tipo del documento: Article País de afiliación: Japón Pais de publicación: Reino Unido
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
Buscar en Google

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Burkholderia / Lipasa Idioma: En Revista: FEBS Lett Año: 2024 Tipo del documento: Article País de afiliación: Japón Pais de publicación: Reino Unido