2018 journal article

Diacylglycerol acyltransferase 1 is activated by phosphatidate and inhibited by SnRK1-catalyzed phosphorylation

PLANT JOURNAL, 96(2), 287–299.

By: K. Caldo*, W. Shen n, Y. Xu*, L. Hanley-Bowdoin n, G. Chen*, R. Weselake*, M. Lemieux*

author keywords: triacylglycerol biosynthesis; DGAT; Brassica napus; biochemical regulation; allostery
MeSH headings : Acyl Coenzyme A / metabolism; Brassica napus / enzymology; Brassica napus / genetics; Carbohydrate Metabolism; Catalysis; Diacylglycerol O-Acyltransferase / genetics; Diacylglycerol O-Acyltransferase / metabolism; Energy Metabolism; Homeostasis; Lipids / physiology; Phosphatidic Acids / metabolism; Phosphorylation; Plant Proteins / genetics; Plant Proteins / metabolism; Protein Serine-Threonine Kinases / genetics; Protein Serine-Threonine Kinases / metabolism; Triglycerides / biosynthesis
TL;DR: Phosphatidate (PA) was identified as a feed-forward activator of BnaDGAT1, enabling the final enzyme in the Kennedy pathway to adjust to the incoming flow of carbon leading to TAG, indicating that PA facilitates the transition of the enzyme into the more active state. (via Semantic Scholar)
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Source: Web Of Science
Added: October 22, 2018

Summary