Physiological role of yeasts NAD(P)+ and NADP+-linked aldehyde dehydrogenases
The activity of NAD+ and NADP+-linked aldehyde dehydrogenases has been investigated in yeast cells grown under different conditions. As occurs in other dehydrogenase reactions the NAD(P)+-linked enzyme was strongly repressed in all hypoxic conditions; nervetheless, the NADP+-linked enzyme was active. The results suggest that the NAD(P)+ aldehyde dehydrogenase is involved in the oxidation of ethanol to acetyl-CoA, and that when the pyruvate dehydrogenase complex is repressed the NADP+-linked aldehyde dehydrogenase is operative as an alternative pathway from pyruvate to acetyl-CoA: pyruvate leads to acetaldehyde leads to acetate leads to acetyl-Coa. In these conditions the supply of NADPH is advantageous to the cellular economy for biosynthetic purposes. Short term adaptation experiments suggest that the regulation of the levels of the aldehyde dehydrogenase-NAD(P)+ takes place by the de novo synthesis of the enzyme.
Medienart: |
Artikel |
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Erscheinungsjahr: |
1977 |
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Erschienen: |
1977 |
Enthalten in: |
Zur Gesamtaufnahme - volume:33 |
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Enthalten in: |
Revista espanola de fisiologia - 33(1977), 2 vom: 15. Juni, Seite 135-42 |
Sprache: |
Englisch |
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Beteiligte Personen: |
Llorente, N [VerfasserIn] |
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Themen: |
0U46U6E8UK |
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Anmerkungen: |
Date Completed 25.08.1977 Date Revised 21.11.2013 published: Print Citation Status MEDLINE |
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Förderinstitution / Projekttitel: |
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PPN (Katalog-ID): |
NLM000187534 |
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245 | 1 | 0 | |a Physiological role of yeasts NAD(P)+ and NADP+-linked aldehyde dehydrogenases |
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500 | |a Date Completed 25.08.1977 | ||
500 | |a Date Revised 21.11.2013 | ||
500 | |a published: Print | ||
500 | |a Citation Status MEDLINE | ||
520 | |a The activity of NAD+ and NADP+-linked aldehyde dehydrogenases has been investigated in yeast cells grown under different conditions. As occurs in other dehydrogenase reactions the NAD(P)+-linked enzyme was strongly repressed in all hypoxic conditions; nervetheless, the NADP+-linked enzyme was active. The results suggest that the NAD(P)+ aldehyde dehydrogenase is involved in the oxidation of ethanol to acetyl-CoA, and that when the pyruvate dehydrogenase complex is repressed the NADP+-linked aldehyde dehydrogenase is operative as an alternative pathway from pyruvate to acetyl-CoA: pyruvate leads to acetaldehyde leads to acetate leads to acetyl-Coa. In these conditions the supply of NADPH is advantageous to the cellular economy for biosynthetic purposes. Short term adaptation experiments suggest that the regulation of the levels of the aldehyde dehydrogenase-NAD(P)+ takes place by the de novo synthesis of the enzyme | ||
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