Publikationen - Molekulare Signalverarbeitung
Aktive Filter
Autor Nach Häufigkeit alphabetisch sortiert: Monostori, T
Autor Nach Häufigkeit alphabetisch sortiert: Wasternack, C
Autor Nach Häufigkeit alphabetisch sortiert: Maucher, H
Autor Nach Häufigkeit alphabetisch sortiert: Wasternack, C.
Journal / Buchreihe / Preprint-Server Nach Häufigkeit alphabetisch sortiert: Biologie in unserer Zeit
Journal / Buchreihe / Preprint-Server Nach Häufigkeit alphabetisch sortiert: Biol. Chem
Journal / Buchreihe / Preprint-Server Nach Häufigkeit alphabetisch sortiert: Plant Signal Behav
Autor Nach Häufigkeit alphabetisch sortiert: Mitra, D.
Journal / Buchreihe / Preprint-Server Nach Häufigkeit alphabetisch sortiert: FEBS Lett.
Erscheinungsjahr: 2007
Alle Filter entfernen
Suchfilter
- Typ der Publikation
- Publikation (1)
- Erscheinungsjahr
- Journal / Buchreihe / Preprint-Server Nach Häufigkeit alphabetisch sortiert
- 0 (1)
- Ann. Bot. (1)
- Biol. Chem. (1)
- FEBS Lett. (1)
- J. Exp. Bot. (1)
- Phytochemistry (1)
- Phytomedicine (1)
- Plant Cell Physiol. (1)
- Plant Mol. Biol. (1)
- Autor Nach Häufigkeit alphabetisch sortiert
- Guranowski, A. (1)
- Miersch, O. (1)
- Staswick, P. E. (1)
- Suza, W. (1)
- Wasternack, C. (1)
Zeige Ergebnisse 1 bis 1 von 1.
Guranowski, A.; Miersch, O.; Staswick, P. E.; Suza, W.; Wasternack, C.; Substrate specificity and products of side-reactions catalyzed by jasmonate:amino acid synthetase (JAR1) FEBS Lett. 581, 815-820, (2007) DOI: 10.1016/j.febslet.2007.01.049
Jasmonate:amino acid synthetase (JAR1) is involved in the function of jasmonic acid (JA) as a plant hormone. It catalyzes the synthesis of several JA‐amido conjugates, the most important of which appears to be JA‐Ile. Structurally, JAR1 is a member of the firefly luciferase superfamily that comprises enzymes that adenylate various organic acids. This study analyzed the substrate specificity of recombinant JAR1 and determined whether it catalyzes the synthesis of mono‐ and dinucleoside polyphosphates, which are side‐reaction products of many enzymes forming acyl ∼ adenylates. Among different oxylipins tested as mixed stereoisomers for substrate activity with JAR1, the highest rate of conversion to Ile‐conjugates was observed for (±)‐JA and 9,10‐dihydro‐JA, while the rate of conjugation with 12‐hydroxy‐JA and OPC‐4 (3‐oxo‐2‐(2Z ‐pentenyl)cyclopentane‐1‐butyric acid) was only about 1–2% that for (±)‐JA. Of the two stereoisomers of JA, (−)‐JA and (+)‐JA, rate of synthesis of the former was about 100‐fold faster than for (+)‐JA. Finally, we have demonstrated that (1) in the presence of ATP, Mg2+, (−)‐JA and tripolyphosphate the ligase produces adenosine 5′‐tetraphosphate (p4A); (2) addition of isoleucine to that mixture halts the p4A synthesis; (3) the enzyme produces neither diadenosine triphosphate (Ap3A) nor diadenosine tetraphosphate (Ap4A) and (4) Ap4A cannot substitute ATP as a source of adenylate in the complete reaction that yields JA‐Ile.