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Mutations of Thr169 affect substrate specificity of pyranose 2-oxidase from Trametes multicolor
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2008 (English)In: Biocatalysis and Biotransformation, ISSN 1024-2422, E-ISSN 1029-2446, Vol. 26, no 1-2, 120-127 p.Article in journal (Refereed) Published
Abstract [en]

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.

Place, publisher, year, edition, pages
2008. Vol. 26, no 1-2, 120-127 p.
Keyword [en]
pyranose oxidase, enzyme engineering, substrate specificity, galactose, oxidation, electron-transfer flavoprotein, phanerochaete-chrysosporium, reaction-products, d-glucose, oxidase, purification, binding, enzyme, oxidation, design
Identifiers
URN: urn:nbn:se:kth:diva-17352DOI: 10.1080/10242420701789320ISI: 000253658000016Scopus ID: 2-s2.0-50549091341OAI: oai:DiVA.org:kth-17352DiVA: diva2:335396
Note
QC 20100525Available from: 2010-08-05 Created: 2010-08-05 Last updated: 2017-12-12Bibliographically approved

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Divne, Christina

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