BOKU - Universität für Bodenkultur Wien - Forschungsinformationssystem

Logo BOKU-Forschungsportal

Gewählte Publikation:

Spadiut, O., Leitner, C., Tan, T.-C., Ludwig, R., Divne, C., Haltrich, D..
(2008): Mutations of Thr169 affect substrate specificity of pyranose 2-oxidase from Trametes multicolor
BIOCATAL BIOTRANSFOR, 26, 120-127; ISSN 1024-2422 FullText FullText_BOKU

Site-directed mutagenesis was used to enhance the catalytic activity of pyranose 2-oxidase (P2Ox) from Trametes multicolor with different substrates. To this end, threonine at position 169 was replaced by glycine, alanine and serine, respectively. Using oxygen as electron acceptor the mutant T169G was equally active with d-glucose and d-galactose, whereas wild-type recombinant P2Ox only showed 5.2% relative activity with the latter substrate. When d-galactose was used as electron donor in saturating concentrations, T169G showed a 4.5-fold increase in its catalytic efficiency k(cat)/K-M for the alternative electron acceptor 1,4-benzoquinone and a nine-fold increased k(cat)/K-M value with the ferricenium ion compared with wt recP2Ox. Variant T169S showed an increase in its catalytic efficiency both with 1,4-benzoquinone (3.7 times) as well as with the ferricenium ion (1.4 times) when D-glucose was the substrate.
Autor/innen der BOKU Wien:
Haltrich Dietmar
Leitner Christian
Ludwig Roland
BOKU Gendermonitor:

Find related publications in this database (Keywords)
pyranose oxidase
enzyme engineering
substrate specificity
galactose oxidation

© BOKU Wien Impressum