Phosphoserine is the phosphorylated ester of the amino acid serine. The addition of a phosphoryl group to an amino acid, or its removal, plays a role in cell signaling and metabolism. Phosphoserine is a byproduct of glycolysis and subsequent intermediate to then become serine. The enzyme that catalyzes this step, phosphoserine phosphatase, is magnesium dependent. This metabolite is not to be confused with a similar-sounding metabolite, phosphatidylserine; this is a common CNS supplement and essential for neuronal cell membranes.
- Peeraer Y, Rabijns A, Collet JF, Van Schaftingen E, De Ranter C. How calcium inhibits the magnesium-dependent enzyme human phosphoserine phosphatase. Eur J Biochem. 2004;271(16):3421-3427.
- Kim HY, Huang BX, Spector AA. Phosphatidylserine in the brain: metabolism and function. Prog Lipid Res. 2014;56:1-18.
- Ramos RJ, Pras-Raves ML, Gerrits J, et al. Vitamin B6 is essential for serine de novo biosynthesis. J Inherit Metab Dis. 2017;40(6):883-891.
- Kang-Yoon SA, Kirksey A. Relation of short-term pyridoxineHCl supplementation to plasma vitamin B-6 vitamers and amino acid concentrations in young women. Am J Clin Nutr. 1992;55(4):865-872.
The enzyme which connects glycolysis to the formation of phosphoserine (phosphoserine aminotransferase) requires vitamin B6 as a cofactor. Lack of vitamin B6 can result in lower phosphoserine levels.
Supplementation with vitamin B6 was shown to alter plasma amino acids resulting in increased phosphoserine.
Elevated phosphoserine may be due to a functional lack of magnesium needed to catalyze the enzymatic conversion of phosphoserine to serine.
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