دورية أكاديمية

A Fungal Ascorbate Oxidase with Unexpected Laccase Activity.

التفاصيل البيبلوغرافية
العنوان: A Fungal Ascorbate Oxidase with Unexpected Laccase Activity.
المؤلفون: Braunschmid V; Institute of Environmental Biotechnology, Department of Agrobiotechnology, University of Natural Resources and Life Sciences (BOKU), 3430 Tulln an der Donau, Austria.; Austrian Centre for Industrial Biotechnology (ACIB), 3430 Tulln an der Donau, Austria., Fuerst S; Austrian Centre for Industrial Biotechnology (ACIB), 3430 Tulln an der Donau, Austria., Perz V; Institute of Environmental Biotechnology, Department of Agrobiotechnology, University of Natural Resources and Life Sciences (BOKU), 3430 Tulln an der Donau, Austria., Zitzenbacher S; Institute of Environmental Biotechnology, Department of Agrobiotechnology, University of Natural Resources and Life Sciences (BOKU), 3430 Tulln an der Donau, Austria., Hoyo J; Grup de Biotecnologia Molecular i Industrial, Department d'Enginyeria Química, Universitat Politècnica de Catalunya, Rambla Sant Nebridi, 08222 Terrassa, Spain., Fernandez-Sanchez C; Instituto de Microelectronica de Barcelona (IMB-CNM), CSIC, Campus UAB, 08193 Bellatera, Spain., Tzanov T; Grup de Biotecnologia Molecular i Industrial, Department d'Enginyeria Química, Universitat Politècnica de Catalunya, Rambla Sant Nebridi, 08222 Terrassa, Spain., Steinkellner G; Austrian Centre for Industrial Biotechnology (ACIB), 3430 Tulln an der Donau, Austria.; Innophore GmbH, 8010 Graz, Austria., Gruber K; Austrian Centre for Industrial Biotechnology (ACIB), 3430 Tulln an der Donau, Austria.; Structural Biology, Institute of Molecular Bioscience, University of Graz, 8010 Graz, Austria., Nyanhongo GS; Institute of Environmental Biotechnology, Department of Agrobiotechnology, University of Natural Resources and Life Sciences (BOKU), 3430 Tulln an der Donau, Austria.; Austrian Centre for Industrial Biotechnology (ACIB), 3430 Tulln an der Donau, Austria., Ribitsch D; Institute of Environmental Biotechnology, Department of Agrobiotechnology, University of Natural Resources and Life Sciences (BOKU), 3430 Tulln an der Donau, Austria.; Austrian Centre for Industrial Biotechnology (ACIB), 3430 Tulln an der Donau, Austria., Guebitz GM; Institute of Environmental Biotechnology, Department of Agrobiotechnology, University of Natural Resources and Life Sciences (BOKU), 3430 Tulln an der Donau, Austria.; Austrian Centre for Industrial Biotechnology (ACIB), 3430 Tulln an der Donau, Austria.
المصدر: International journal of molecular sciences [Int J Mol Sci] 2020 Aug 11; Vol. 21 (16). Date of Electronic Publication: 2020 Aug 11.
نوع المنشور: Journal Article
اللغة: English
بيانات الدورية: Publisher: MDPI Country of Publication: Switzerland NLM ID: 101092791 Publication Model: Electronic Cited Medium: Internet ISSN: 1422-0067 (Electronic) Linking ISSN: 14220067 NLM ISO Abbreviation: Int J Mol Sci Subsets: MEDLINE
أسماء مطبوعة: Original Publication: Basel, Switzerland : MDPI, [2000-
مواضيع طبية MeSH: Ascorbate Oxidase/*metabolism , Aspergillus flavus/*enzymology , Laccase/*metabolism, Amino Acid Sequence ; Ascorbate Oxidase/chemistry ; Copper/metabolism ; Kinetics ; Laccase/chemistry ; Models, Molecular ; Oxidation-Reduction ; Substrate Specificity
مستخلص: Ascorbate oxidases are an enzyme group that has not been explored to a large extent. So far, mainly ascorbate oxidases from plants and only a few from fungi have been described. Although ascorbate oxidases belong to the well-studied enzyme family of multi-copper oxidases, their function is still unclear. In this study, Af _AO1, an enzyme from the fungus Aspergillus flavus , was characterized. Sequence analyses and copper content determination demonstrated Af _AO1 to belong to the multi-copper oxidase family. Biochemical characterization and 3D-modeling revealed a similarity to ascorbate oxidases, but also to laccases. Af _AO1 had a 10-fold higher affinity to ascorbic acid ( K M = 0.16 ± 0.03 mM) than to ABTS ( K M = 1.89 ± 0.12 mM). Furthermore, the best fitting 3D-model was based on the ascorbate oxidase from Cucurbita pepo var. melopepo . The laccase-like activity of Af _AO1 on ABTS ( V max = 11.56 ± 0.15 µM/min/mg) was, however, not negligible. On the other hand, other typical laccase substrates, such as syringaldezine and guaiacol, were not oxidized by Af _AO1. According to the biochemical and structural characterization, Af _AO1 was classified as ascorbate oxidase with unusual, laccase-like activity.
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معلومات مُعتمدة: SC16-019 NÖ Forschungs- und Bildungsges.m.b.H.; 872161 Austrian Centre of Industrial Biotechnology; Open Access Publishing Fund Universität für Bodenkultur Wien
فهرسة مساهمة: Keywords: ABTS; ascorbate oxidase; laccase; multi-copper oxidase
المشرفين على المادة: 789U1901C5 (Copper)
EC 1.10.3.2 (Laccase)
EC 1.10.3.3 (Ascorbate Oxidase)
تواريخ الأحداث: Date Created: 20200816 Date Completed: 20210217 Latest Revision: 20210217
رمز التحديث: 20221213
مُعرف محوري في PubMed: PMC7460845
DOI: 10.3390/ijms21165754
PMID: 32796622
قاعدة البيانات: MEDLINE
الوصف
تدمد:1422-0067
DOI:10.3390/ijms21165754