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PDC1, a pyruvate/α‐ketoacid decarboxylase, is involved in acetaldehyde, propanal and pentanal biosynthesis in melon (Cucumis melo L.) fruit
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| Zeitschriftentitel: | The Plant Journal |
|---|---|
| Personen und Körperschaften: | , , , , , |
| In: | The Plant Journal, 98, 2019, 1, S. 112-125 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
Wiley
|
| Schlagwörter: |
| author_facet |
Wang, Minmin Zhang, Lei Boo, Kyung Hwan Park, Eunsook Drakakaki, Georgia Zakharov, Florence Wang, Minmin Zhang, Lei Boo, Kyung Hwan Park, Eunsook Drakakaki, Georgia Zakharov, Florence |
|---|---|
| author |
Wang, Minmin Zhang, Lei Boo, Kyung Hwan Park, Eunsook Drakakaki, Georgia Zakharov, Florence |
| spellingShingle |
Wang, Minmin Zhang, Lei Boo, Kyung Hwan Park, Eunsook Drakakaki, Georgia Zakharov, Florence The Plant Journal PDC1, a pyruvate/α‐ketoacid decarboxylase, is involved in acetaldehyde, propanal and pentanal biosynthesis in melon (Cucumis melo L.) fruit Cell Biology Plant Science Genetics |
| author_sort |
wang, minmin |
| spelling |
Wang, Minmin Zhang, Lei Boo, Kyung Hwan Park, Eunsook Drakakaki, Georgia Zakharov, Florence 0960-7412 1365-313X Wiley Cell Biology Plant Science Genetics http://dx.doi.org/10.1111/tpj.14204 <jats:title>Summary</jats:title><jats:p>Plant pyruvate decarboxylases (<jats:styled-content style="fixed-case">PDC</jats:styled-content>) catalyze the decarboxylation of pyruvate to form acetaldehyde and <jats:styled-content style="fixed-case">CO</jats:styled-content><jats:sub>2</jats:sub> and are well known to play a key role in energy supply via fermentative metabolism in oxygen‐limiting conditions. In addition to their role in fermentation, plant <jats:styled-content style="fixed-case">PDC</jats:styled-content>s have also been hypothesized to be involved in aroma formation although, to date, there is no direct biochemical evidence for this function. We investigated the role of <jats:styled-content style="fixed-case">PDC</jats:styled-content>s in fruit volatile biosynthesis, and identified a melon pyruvate decarboxylase, <jats:italic><jats:styled-content style="fixed-case">PDC</jats:styled-content>1</jats:italic>, that is highly expressed in ripe fruits. <jats:italic>In vitro</jats:italic> biochemical characterization of the recombinant <jats:styled-content style="fixed-case">PDC</jats:styled-content>1 enzyme showed that it could not only decarboxylate pyruvate, but that it also had significant activity toward other straight‐ and branched‐chain α‐ketoacids, greatly expanding the range of substrates previously known to be accepted by the plant enzyme. <jats:styled-content style="fixed-case">RNA</jats:styled-content>i‐mediated transient and stable silencing of <jats:italic><jats:styled-content style="fixed-case">PDC</jats:styled-content>1</jats:italic> expression in melon showed that this gene is involved in acetaldehyde, propanal and pentanal production, while it does not contribute to branched‐chain amino acid (<jats:styled-content style="fixed-case">BCAA</jats:styled-content>)‐derived aldehyde biosynthesis in melon fruit. Importantly, our results not only demonstrate additional functions for the <jats:styled-content style="fixed-case">PDC</jats:styled-content> enzyme, but also challenge the long standing hypothesis that <jats:styled-content style="fixed-case">PDC</jats:styled-content> is involved in <jats:styled-content style="fixed-case">BCAA</jats:styled-content>‐derived aldehyde formation in fruit.</jats:p> <scp>PDC</scp>1, a pyruvate/α‐ketoacid decarboxylase, is involved in acetaldehyde, propanal and pentanal biosynthesis in melon (<i>Cucumis melo</i> L.) fruit The Plant Journal |
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10.1111/tpj.14204 |
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Online Free |
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Biologie |
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ElectronicArticle |
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| imprint |
Wiley, 2019 |
| imprint_str_mv |
Wiley, 2019 |
| issn |
0960-7412 1365-313X |
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0960-7412 1365-313X |
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English |
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wang2019pdc1apyruvateaketoaciddecarboxylaseisinvolvedinacetaldehydepropanalandpentanalbiosynthesisinmeloncucumismelolfruit |
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2019 |
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Wiley |
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ai |
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ai |
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The Plant Journal |
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49 |
| title |
PDC1, a pyruvate/α‐ketoacid decarboxylase, is involved in acetaldehyde, propanal and pentanal biosynthesis in melon (Cucumis melo L.) fruit |
| title_unstemmed |
PDC1, a pyruvate/α‐ketoacid decarboxylase, is involved in acetaldehyde, propanal and pentanal biosynthesis in melon (Cucumis melo L.) fruit |
| title_full |
PDC1, a pyruvate/α‐ketoacid decarboxylase, is involved in acetaldehyde, propanal and pentanal biosynthesis in melon (Cucumis melo L.) fruit |
| title_fullStr |
PDC1, a pyruvate/α‐ketoacid decarboxylase, is involved in acetaldehyde, propanal and pentanal biosynthesis in melon (Cucumis melo L.) fruit |
| title_full_unstemmed |
PDC1, a pyruvate/α‐ketoacid decarboxylase, is involved in acetaldehyde, propanal and pentanal biosynthesis in melon (Cucumis melo L.) fruit |
| title_short |
PDC1, a pyruvate/α‐ketoacid decarboxylase, is involved in acetaldehyde, propanal and pentanal biosynthesis in melon (Cucumis melo L.) fruit |
| title_sort |
<scp>pdc</scp>1, a pyruvate/α‐ketoacid decarboxylase, is involved in acetaldehyde, propanal and pentanal biosynthesis in melon (<i>cucumis melo</i> l.) fruit |
| topic |
Cell Biology Plant Science Genetics |
| url |
http://dx.doi.org/10.1111/tpj.14204 |
| publishDate |
2019 |
| physical |
112-125 |
| description |
<jats:title>Summary</jats:title><jats:p>Plant pyruvate decarboxylases (<jats:styled-content style="fixed-case">PDC</jats:styled-content>) catalyze the decarboxylation of pyruvate to form acetaldehyde and <jats:styled-content style="fixed-case">CO</jats:styled-content><jats:sub>2</jats:sub> and are well known to play a key role in energy supply via fermentative metabolism in oxygen‐limiting conditions. In addition to their role in fermentation, plant <jats:styled-content style="fixed-case">PDC</jats:styled-content>s have also been hypothesized to be involved in aroma formation although, to date, there is no direct biochemical evidence for this function. We investigated the role of <jats:styled-content style="fixed-case">PDC</jats:styled-content>s in fruit volatile biosynthesis, and identified a melon pyruvate decarboxylase, <jats:italic><jats:styled-content style="fixed-case">PDC</jats:styled-content>1</jats:italic>, that is highly expressed in ripe fruits. <jats:italic>In vitro</jats:italic> biochemical characterization of the recombinant <jats:styled-content style="fixed-case">PDC</jats:styled-content>1 enzyme showed that it could not only decarboxylate pyruvate, but that it also had significant activity toward other straight‐ and branched‐chain α‐ketoacids, greatly expanding the range of substrates previously known to be accepted by the plant enzyme. <jats:styled-content style="fixed-case">RNA</jats:styled-content>i‐mediated transient and stable silencing of <jats:italic><jats:styled-content style="fixed-case">PDC</jats:styled-content>1</jats:italic> expression in melon showed that this gene is involved in acetaldehyde, propanal and pentanal production, while it does not contribute to branched‐chain amino acid (<jats:styled-content style="fixed-case">BCAA</jats:styled-content>)‐derived aldehyde biosynthesis in melon fruit. Importantly, our results not only demonstrate additional functions for the <jats:styled-content style="fixed-case">PDC</jats:styled-content> enzyme, but also challenge the long standing hypothesis that <jats:styled-content style="fixed-case">PDC</jats:styled-content> is involved in <jats:styled-content style="fixed-case">BCAA</jats:styled-content>‐derived aldehyde formation in fruit.</jats:p> |
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| author | Wang, Minmin, Zhang, Lei, Boo, Kyung Hwan, Park, Eunsook, Drakakaki, Georgia, Zakharov, Florence |
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| description | <jats:title>Summary</jats:title><jats:p>Plant pyruvate decarboxylases (<jats:styled-content style="fixed-case">PDC</jats:styled-content>) catalyze the decarboxylation of pyruvate to form acetaldehyde and <jats:styled-content style="fixed-case">CO</jats:styled-content><jats:sub>2</jats:sub> and are well known to play a key role in energy supply via fermentative metabolism in oxygen‐limiting conditions. In addition to their role in fermentation, plant <jats:styled-content style="fixed-case">PDC</jats:styled-content>s have also been hypothesized to be involved in aroma formation although, to date, there is no direct biochemical evidence for this function. We investigated the role of <jats:styled-content style="fixed-case">PDC</jats:styled-content>s in fruit volatile biosynthesis, and identified a melon pyruvate decarboxylase, <jats:italic><jats:styled-content style="fixed-case">PDC</jats:styled-content>1</jats:italic>, that is highly expressed in ripe fruits. <jats:italic>In vitro</jats:italic> biochemical characterization of the recombinant <jats:styled-content style="fixed-case">PDC</jats:styled-content>1 enzyme showed that it could not only decarboxylate pyruvate, but that it also had significant activity toward other straight‐ and branched‐chain α‐ketoacids, greatly expanding the range of substrates previously known to be accepted by the plant enzyme. <jats:styled-content style="fixed-case">RNA</jats:styled-content>i‐mediated transient and stable silencing of <jats:italic><jats:styled-content style="fixed-case">PDC</jats:styled-content>1</jats:italic> expression in melon showed that this gene is involved in acetaldehyde, propanal and pentanal production, while it does not contribute to branched‐chain amino acid (<jats:styled-content style="fixed-case">BCAA</jats:styled-content>)‐derived aldehyde biosynthesis in melon fruit. Importantly, our results not only demonstrate additional functions for the <jats:styled-content style="fixed-case">PDC</jats:styled-content> enzyme, but also challenge the long standing hypothesis that <jats:styled-content style="fixed-case">PDC</jats:styled-content> is involved in <jats:styled-content style="fixed-case">BCAA</jats:styled-content>‐derived aldehyde formation in fruit.</jats:p> |
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| spelling | Wang, Minmin Zhang, Lei Boo, Kyung Hwan Park, Eunsook Drakakaki, Georgia Zakharov, Florence 0960-7412 1365-313X Wiley Cell Biology Plant Science Genetics http://dx.doi.org/10.1111/tpj.14204 <jats:title>Summary</jats:title><jats:p>Plant pyruvate decarboxylases (<jats:styled-content style="fixed-case">PDC</jats:styled-content>) catalyze the decarboxylation of pyruvate to form acetaldehyde and <jats:styled-content style="fixed-case">CO</jats:styled-content><jats:sub>2</jats:sub> and are well known to play a key role in energy supply via fermentative metabolism in oxygen‐limiting conditions. In addition to their role in fermentation, plant <jats:styled-content style="fixed-case">PDC</jats:styled-content>s have also been hypothesized to be involved in aroma formation although, to date, there is no direct biochemical evidence for this function. We investigated the role of <jats:styled-content style="fixed-case">PDC</jats:styled-content>s in fruit volatile biosynthesis, and identified a melon pyruvate decarboxylase, <jats:italic><jats:styled-content style="fixed-case">PDC</jats:styled-content>1</jats:italic>, that is highly expressed in ripe fruits. <jats:italic>In vitro</jats:italic> biochemical characterization of the recombinant <jats:styled-content style="fixed-case">PDC</jats:styled-content>1 enzyme showed that it could not only decarboxylate pyruvate, but that it also had significant activity toward other straight‐ and branched‐chain α‐ketoacids, greatly expanding the range of substrates previously known to be accepted by the plant enzyme. <jats:styled-content style="fixed-case">RNA</jats:styled-content>i‐mediated transient and stable silencing of <jats:italic><jats:styled-content style="fixed-case">PDC</jats:styled-content>1</jats:italic> expression in melon showed that this gene is involved in acetaldehyde, propanal and pentanal production, while it does not contribute to branched‐chain amino acid (<jats:styled-content style="fixed-case">BCAA</jats:styled-content>)‐derived aldehyde biosynthesis in melon fruit. Importantly, our results not only demonstrate additional functions for the <jats:styled-content style="fixed-case">PDC</jats:styled-content> enzyme, but also challenge the long standing hypothesis that <jats:styled-content style="fixed-case">PDC</jats:styled-content> is involved in <jats:styled-content style="fixed-case">BCAA</jats:styled-content>‐derived aldehyde formation in fruit.</jats:p> <scp>PDC</scp>1, a pyruvate/α‐ketoacid decarboxylase, is involved in acetaldehyde, propanal and pentanal biosynthesis in melon (<i>Cucumis melo</i> L.) fruit The Plant Journal |
| spellingShingle | Wang, Minmin, Zhang, Lei, Boo, Kyung Hwan, Park, Eunsook, Drakakaki, Georgia, Zakharov, Florence, The Plant Journal, PDC1, a pyruvate/α‐ketoacid decarboxylase, is involved in acetaldehyde, propanal and pentanal biosynthesis in melon (Cucumis melo L.) fruit, Cell Biology, Plant Science, Genetics |
| title | PDC1, a pyruvate/α‐ketoacid decarboxylase, is involved in acetaldehyde, propanal and pentanal biosynthesis in melon (Cucumis melo L.) fruit |
| title_full | PDC1, a pyruvate/α‐ketoacid decarboxylase, is involved in acetaldehyde, propanal and pentanal biosynthesis in melon (Cucumis melo L.) fruit |
| title_fullStr | PDC1, a pyruvate/α‐ketoacid decarboxylase, is involved in acetaldehyde, propanal and pentanal biosynthesis in melon (Cucumis melo L.) fruit |
| title_full_unstemmed | PDC1, a pyruvate/α‐ketoacid decarboxylase, is involved in acetaldehyde, propanal and pentanal biosynthesis in melon (Cucumis melo L.) fruit |
| title_short | PDC1, a pyruvate/α‐ketoacid decarboxylase, is involved in acetaldehyde, propanal and pentanal biosynthesis in melon (Cucumis melo L.) fruit |
| title_sort | <scp>pdc</scp>1, a pyruvate/α‐ketoacid decarboxylase, is involved in acetaldehyde, propanal and pentanal biosynthesis in melon (<i>cucumis melo</i> l.) fruit |
| title_unstemmed | PDC1, a pyruvate/α‐ketoacid decarboxylase, is involved in acetaldehyde, propanal and pentanal biosynthesis in melon (Cucumis melo L.) fruit |
| topic | Cell Biology, Plant Science, Genetics |
| url | http://dx.doi.org/10.1111/tpj.14204 |