A Fungal Ascorbate Oxidase with Unexpected Laccase Activity
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 unc...
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| Veröffentlicht in: | International journal of molecular sciences 2020-08, Vol.21 (16), p.5754 |
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| creator | Braunschmid, Verena Fuerst, Sarah Perz, Veronika Zitzenbacher, Sabine Hoyo, Javier Fernandez-Sanchez, Cesar Tzanov, Tzanko Steinkellner, Georg Gruber, Karl Nyanhongo, Gibson S Ribitsch, Doris Guebitz, Georg M |
| description | 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,
_AO1, an enzyme from the fungus
, was characterized. Sequence analyses and copper content determination demonstrated
_AO1 to belong to the multi-copper oxidase family. Biochemical characterization and 3D-modeling revealed a similarity to ascorbate oxidases, but also to laccases.
_AO1 had a 10-fold higher affinity to ascorbic acid (
= 0.16 ± 0.03 mM) than to ABTS (
= 1.89 ± 0.12 mM). Furthermore, the best fitting 3D-model was based on the ascorbate oxidase from
var.
. The laccase-like activity of
_AO1 on ABTS (
= 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
_AO1. According to the biochemical and structural characterization,
_AO1 was classified as ascorbate oxidase with unusual, laccase-like activity. |
| doi_str_mv | 10.3390/ijms21165754 |
| format | Article |
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_AO1, an enzyme from the fungus
, was characterized. Sequence analyses and copper content determination demonstrated
_AO1 to belong to the multi-copper oxidase family. Biochemical characterization and 3D-modeling revealed a similarity to ascorbate oxidases, but also to laccases.
_AO1 had a 10-fold higher affinity to ascorbic acid (
= 0.16 ± 0.03 mM) than to ABTS (
= 1.89 ± 0.12 mM). Furthermore, the best fitting 3D-model was based on the ascorbate oxidase from
var.
. The laccase-like activity of
_AO1 on ABTS (
= 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
_AO1. According to the biochemical and structural characterization,
_AO1 was classified as ascorbate oxidase with unusual, laccase-like activity.</description><identifier>ISSN: 1422-0067</identifier><identifier>ISSN: 1661-6596</identifier><identifier>EISSN: 1422-0067</identifier><identifier>DOI: 10.3390/ijms21165754</identifier><identifier>PMID: 32796622</identifier><language>eng</language><publisher>Switzerland: MDPI AG</publisher><subject>Amino Acid Sequence ; Ascorbate oxidase ; Ascorbate Oxidase - chemistry ; Ascorbate Oxidase - metabolism ; Ascorbic acid ; Aspergillus flavus ; Aspergillus flavus - enzymology ; Binding sites ; Copper - metabolism ; Enzyme kinetics ; Fungi ; Genomes ; Guaiacol ; Kinetics ; L-Ascorbate oxidase ; Laccase ; Laccase - chemistry ; Laccase - metabolism ; Models, Molecular ; Multicopper oxidase ; Oxidation ; Oxidation-Reduction ; Proteins ; Structural analysis ; Substrate Specificity ; Vitamin C</subject><ispartof>International journal of molecular sciences, 2020-08, Vol.21 (16), p.5754</ispartof><rights>2020. This work is licensed under http://creativecommons.org/licenses/by/3.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2020 by the authors. 2020</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c412t-684a9b7c1a845e61820f68a91e5b8b162f2d40d363e9a2ff60560346c051f9be3</citedby><cites>FETCH-LOGICAL-c412t-684a9b7c1a845e61820f68a91e5b8b162f2d40d363e9a2ff60560346c051f9be3</cites><orcidid>0000-0002-4951-2547 ; 0000-0003-2262-487X ; 0000-0002-8568-1110</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC7460845/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC7460845/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,881,27901,27902,53766,53768</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/32796622$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Braunschmid, Verena</creatorcontrib><creatorcontrib>Fuerst, Sarah</creatorcontrib><creatorcontrib>Perz, Veronika</creatorcontrib><creatorcontrib>Zitzenbacher, Sabine</creatorcontrib><creatorcontrib>Hoyo, Javier</creatorcontrib><creatorcontrib>Fernandez-Sanchez, Cesar</creatorcontrib><creatorcontrib>Tzanov, Tzanko</creatorcontrib><creatorcontrib>Steinkellner, Georg</creatorcontrib><creatorcontrib>Gruber, Karl</creatorcontrib><creatorcontrib>Nyanhongo, Gibson S</creatorcontrib><creatorcontrib>Ribitsch, Doris</creatorcontrib><creatorcontrib>Guebitz, Georg M</creatorcontrib><title>A Fungal Ascorbate Oxidase with Unexpected Laccase Activity</title><title>International journal of molecular sciences</title><addtitle>Int J Mol Sci</addtitle><description>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,
_AO1, an enzyme from the fungus
, was characterized. Sequence analyses and copper content determination demonstrated
_AO1 to belong to the multi-copper oxidase family. Biochemical characterization and 3D-modeling revealed a similarity to ascorbate oxidases, but also to laccases.
_AO1 had a 10-fold higher affinity to ascorbic acid (
= 0.16 ± 0.03 mM) than to ABTS (
= 1.89 ± 0.12 mM). Furthermore, the best fitting 3D-model was based on the ascorbate oxidase from
var.
. The laccase-like activity of
_AO1 on ABTS (
= 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
_AO1. According to the biochemical and structural characterization,
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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,
_AO1, an enzyme from the fungus
, was characterized. Sequence analyses and copper content determination demonstrated
_AO1 to belong to the multi-copper oxidase family. Biochemical characterization and 3D-modeling revealed a similarity to ascorbate oxidases, but also to laccases.
_AO1 had a 10-fold higher affinity to ascorbic acid (
= 0.16 ± 0.03 mM) than to ABTS (
= 1.89 ± 0.12 mM). Furthermore, the best fitting 3D-model was based on the ascorbate oxidase from
var.
. The laccase-like activity of
_AO1 on ABTS (
= 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
_AO1. According to the biochemical and structural characterization,
_AO1 was classified as ascorbate oxidase with unusual, laccase-like activity.</abstract><cop>Switzerland</cop><pub>MDPI AG</pub><pmid>32796622</pmid><doi>10.3390/ijms21165754</doi><orcidid>https://orcid.org/0000-0002-4951-2547</orcidid><orcidid>https://orcid.org/0000-0003-2262-487X</orcidid><orcidid>https://orcid.org/0000-0002-8568-1110</orcidid><oa>free_for_read</oa></addata></record> |
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| ispartof | International journal of molecular sciences, 2020-08, Vol.21 (16), p.5754 |
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| source | MDPI - Multidisciplinary Digital Publishing Institute; MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central |
| subjects | Amino Acid Sequence Ascorbate oxidase Ascorbate Oxidase - chemistry Ascorbate Oxidase - metabolism Ascorbic acid Aspergillus flavus Aspergillus flavus - enzymology Binding sites Copper - metabolism Enzyme kinetics Fungi Genomes Guaiacol Kinetics L-Ascorbate oxidase Laccase Laccase - chemistry Laccase - metabolism Models, Molecular Multicopper oxidase Oxidation Oxidation-Reduction Proteins Structural analysis Substrate Specificity Vitamin C |
| title | A Fungal Ascorbate Oxidase with Unexpected Laccase Activity |
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