Biochemical Characterization of 13-Lipoxygenases of Arabidopsis thaliana

Maynard D, Chibani K, Schmidtpott S, Seidel T, Sproß J, Viehhauser A, Dietz K-J (2021)
International Journal of Molecular Sciences 22(19): 10237.

Zeitschriftenaufsatz | Veröffentlicht | Englisch
 
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Abstract / Bemerkung
13-lipoxygenases (13-LOX) catalyze the dioxygenation of various polyunsaturated fatty acids (PUFAs), of which α-linolenic acid (LeA) is converted to 13-S-hydroperoxyoctadeca-9, 11, 15-trienoic acid (13-HPOT), the precursor for the prostaglandin-like plant hormones cis-(+)-12-oxophytodienoic acid (12-OPDA) and methyl jasmonate (MJ). This study aimed for characterizing the four annotated A. thaliana 13-LOX enzymes (LOX2, LOX3, LOX4, and LOX6) focusing on synthesis of 12-OPDA and 4Z,7Z,10Z)-12-[[-(1S,5S)-4-oxo-5-(2Z)-pent-2-en-1yl] cyclopent-2-en-1yl] dodeca-4,7,10-trienoic acid (OCPD). In addition, we performed interaction studies of 13-LOXs with ions and molecules to advance our understanding of 13-LOX. Cell imaging indicated plastid targeting of fluorescent proteins fused to 13-LOXs-N-terminal extensions, supporting the prediction of 13-LOX localization to plastids. The apparent maximal velocity (Vmax app) values for LOX-catalyzed LeA oxidation were highest for LOX4 (128 nmol·s−1·mg protein−1), with a Km value of 5.8 µM. A. thaliana 13-LOXs, in cascade with 12-OPDA pathway enzymes, synthesized 12-OPDA and OCPD from LeA and docosahexaenoic acid, previously shown only for LOX6. The activities of the four isoforms were differently affected by physiologically relevant chemicals, such as Mg2+, Ca2+, Cu2+ and Cd2+, and by 12-OPDA and MJ. As demonstrated for LOX4, 12-OPDA inhibited enzymatic LeA hydroperoxidation, with half-maximal enzyme inhibition at 48 µM. Biochemical interactions, such as the sensitivity of LOX toward thiol-reactive agents belonging to cyclopentenone prostaglandins, are suggested to occur in human LOX homologs. Furthermore, we conclude that 13-LOXs are isoforms with rather specific functional and regulatory enzymatic features.
Stichworte
Arabidopsis thaliana; lipoxygenases; polyunsaturated fatty acids; lipoxygenase inhibitor; oxylipin
Erscheinungsjahr
2021
Zeitschriftentitel
International Journal of Molecular Sciences
Band
22
Ausgabe
19
Art.-Nr.
10237
eISSN
1422-0067
Finanzierungs-Informationen
Open-Access-Publikationskosten wurden durch die Universität Bielefeld gefördert.
Page URI
https://pub.uni-bielefeld.de/record/2957883

Zitieren

Maynard D, Chibani K, Schmidtpott S, et al. Biochemical Characterization of 13-Lipoxygenases of Arabidopsis thaliana. International Journal of Molecular Sciences. 2021;22(19): 10237.
Maynard, D., Chibani, K., Schmidtpott, S., Seidel, T., Sproß, J., Viehhauser, A., & Dietz, K. - J. (2021). Biochemical Characterization of 13-Lipoxygenases of Arabidopsis thaliana. International Journal of Molecular Sciences, 22(19), 10237. https://doi.org/10.3390/ijms221910237
Maynard, D., Chibani, K., Schmidtpott, S., Seidel, T., Sproß, J., Viehhauser, A., and Dietz, K. - J. (2021). Biochemical Characterization of 13-Lipoxygenases of Arabidopsis thaliana. International Journal of Molecular Sciences 22:10237.
Maynard, D., et al., 2021. Biochemical Characterization of 13-Lipoxygenases of Arabidopsis thaliana. International Journal of Molecular Sciences, 22(19): 10237.
D. Maynard, et al., “Biochemical Characterization of 13-Lipoxygenases of Arabidopsis thaliana”, International Journal of Molecular Sciences, vol. 22, 2021, : 10237.
Maynard, D., Chibani, K., Schmidtpott, S., Seidel, T., Sproß, J., Viehhauser, A., Dietz, K.-J.: Biochemical Characterization of 13-Lipoxygenases of Arabidopsis thaliana. International Journal of Molecular Sciences. 22, : 10237 (2021).
Maynard, Daniel, Chibani, Kamel, Schmidtpott, Sonja, Seidel, Thorsten, Sproß, Jens, Viehhauser, Andrea, and Dietz, Karl-Josef. “Biochemical Characterization of 13-Lipoxygenases of Arabidopsis thaliana”. International Journal of Molecular Sciences 22.19 (2021): 10237.
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2021-10-04T08:50:35Z
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