Biochemical Characterization of Acyl‑CoA: Lysophosphatidylcholine Acyltransferase (LPCAT) Enzyme from the Seeds of Salvia hispanica.

Salvia hispanica (chia) is the highest reported terrestrial plant source of alpha-linolenic acid (ALA, ~ 65%), an ω-3 polyunsaturated
fatty acid with numerous health benefits. The molecular basis of high ALA accumulation in chia is yet to be understood.
We have identified lysophosphatidylcholine acyltransferase (LPCAT ) gene from the developing seed transcriptome
data of chia and carried out its biochemical characterization through heterologous expression in Saccharomyces cerevisiae.
Expression profiling showed that the enzyme was active throughout the seed development, indicating a pivotal role in oil
biosynthesis. The enzyme could utilize both saturated and unsaturated lysophosphatidylcholine substrates at the same rate,
to synthesize phosphatidylcholine (PC). The enzyme also exhibited lysophosphatidic acid acyltransferase (LPAAT) activity,
by preferring lysophosphatidic acid substrate. Substrate specificity studies showed that the enzyme preferred both monounsaturated
and polyunsaturated fatty acyl CoAs over saturated CoAs. This activity may play a key role in enriching the
PC fraction with polyunsaturated fatty acids (PUFAs). PUFAs present on PC can be transferred to oil through the action of
other acyltransferases. Our results describe a new LPCAT enzyme that can be used to biotechnologically alter oilseed crops
to incorporate more PUFA in its seed oil.