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Application of a Mass Spectrometric Approach to Detect the Presence of Fatty Acid Biosynthetic Phosphopeptides

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Abstract

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.

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Abbreviations

NLMS3 :

Neutral loss-triggered MS/MS/MS

SRM:

Selected reaction monitoring

ACP:

Acyl-carrier protein

NADP:

Nicotinamide adenine dinucleotide phosphate

ATP:

Adenosine triphosphate

FA:

Formic acid

ACN:

Acetonitrile

CID:

Collision-induced dissociation

TOF:

Time-of-flight

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Acknowledgments

The author would like to thank the Director-General of Malaysian Palm Oil Board for the permission to publish this manuscript. The author also thanks the Malaysian Palm Oil Board for providing the Ph.D. scholarship, project funding and oil palm fruit samples. The author also wishes to acknowledge AgResearch Lincoln Research Centre for the use of their research facilities.

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Correspondence to Benjamin Yii Chung Lau.

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Lau, B.Y.C., Clerens, S., Morton, J.D. et al. Application of a Mass Spectrometric Approach to Detect the Presence of Fatty Acid Biosynthetic Phosphopeptides. Protein J 35, 163–170 (2016). https://doi.org/10.1007/s10930-016-9655-0

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