AgResearch
Browse

File(s) not publicly available

Application of a mass spectrometric approach to detect the presence of fatty acid biosynthetic phosphopeptides

journal contribution
posted on 2023-05-03, 20:32 authored by Benjamin Lau, Stefan ClerensStefan Clerens, James Morton, Jolon Dyer, Santanu Deb-Choudhury, Umi Ramli
The details of plant lipid metabolism are relatively well known but the regulation of fatty acid production at the protein level is still not understood. Hence this study explores the importance of phosphorylation as a mechanism to control the activity of fatty acid biosynthetic enzymes using low and high oleic acid mesocarps of oil palm fruit (Elaeis guineensis variety of Tenera). Adaptation of neutral loss-triggered tandem mass spectrometry and selected reaction monitoring to detect the neutral loss of phosphoric acid successfully found several phosphoamino acid-containing peptides. These peptides corresponded to the peptides from acetyl-CoA carboxylase and 3-enoyl-acyl carrier protein reductase as identified by their precursor ion masses. These findings suggest that these enzymes were phosphorylated at 20th week after anthesis. Phosphorylation could have reduce their activities towards the end of fatty acid biosynthesis at ripening stage. Implication of phosphorylation in the regulation of fatty acid biosynthesis at protein level has never been reported.

History

Rights statement

© Springer Science+Business Media New York 2016

Language

  • English

Does this contain Māori information or data?

  • No

Publisher

Springer International Publishing

Journal title

The Protein Journal

ISSN

1572-3887

Citation

Lau, B. Y., Clerens, S., Morton, J. D., Dyer, J. M., Deb-Choudhury, S., & Ramli, U. S. (2016). Application of a mass spectrometric approach to detect the presence of fatty acid biosynthetic phosphopeptides. The Protein Journal, 35(2), 163-170. doi:10.1007/s10930-016-9655-0

Report number

FBP 56438

Usage metrics

    Exports

    RefWorks
    BibTeX
    Ref. manager
    Endnote
    DataCite
    NLM
    DC