Nitrogen recycling during phenylpropanoid metabolism in sweet potato tubers
In the first step of the phenylpropanoid metabolic pathway, L-phenylalanine (L-Phe) is deaminated to form E-cinnamate, in a conversion catalyzed by phenylalanine ammonia-lyase (PAL; EC 4.3.1.5). The metabolic fate of the ammonium ion (NH4+) produced in this reaction was investigated in sweet potato...
Veröffentlicht in: | Journal of plant physiology. - 1979. - 153(1998), 3-4 vom: 31. Okt., Seite 316-23 |
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1. Verfasser: | |
Weitere Verfasser: | , |
Format: | Aufsatz |
Sprache: | English |
Veröffentlicht: |
1998
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Zugriff auf das übergeordnete Werk: | Journal of plant physiology |
Schlagworte: | Journal Article Research Support, U.S. Gov't, Non-P.H.S. NASA Discipline Plant Biology Non-NASA Center Enzyme Inhibitors Indans Nitrogen Isotopes Quaternary Ammonium Compounds Ammonium Chloride 01Q9PC255D mehr... |
Zusammenfassung: | In the first step of the phenylpropanoid metabolic pathway, L-phenylalanine (L-Phe) is deaminated to form E-cinnamate, in a conversion catalyzed by phenylalanine ammonia-lyase (PAL; EC 4.3.1.5). The metabolic fate of the ammonium ion (NH4+) produced in this reaction was investigated in sweet potato (Ipomoea batatas) tuber discs. [15N]-Labeled substrates including L-Phe, in the presence or absence of specific enzyme inhibitors, were administered to sweet potato discs in light under aseptic conditions. 15N-Nuclear magnetic resonance spectroscopic analyses revealed that the 15NH4+ liberated during the PAL reaction is first incorporated into the amide nitrogen of L-glutamine (L-Gln) and then into L-glutamate (L-Glu). These results extend our previous observations in pine and potato that PAL-generated NH4+ is assimilated by the glutamine synthetase (GS; EC 6.3.1.2)/glutamate synthase (GOGAT; EC 1.4.1.13) pathway, with the NH4+ so formed ultimately being recycled back to L-Phe via L-Glu as aminoreceptor and donor |
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Beschreibung: | Date Completed 25.03.2000 Date Revised 30.09.2020 published: Print Citation Status MEDLINE |
ISSN: | 0176-1617 |