Title : Glycolytic flux controls D-serine synthesis through glyceraldehyde-3-phosphate dehydrogenase in astrocytes.

Pub. Date : 2015 Apr 28

PMID : 25870284






5 Functional Relationships(s)
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1 Here we show that d-serine production in astrocytes is modulated by the interaction between the D-serine synthetic enzyme serine racemase (SRR) and a glycolytic enzyme, glyceraldehyde 3-phosphate dehydrogenase (GAPDH). D-serine serine racemase Homo sapiens
2 Here we show that d-serine production in astrocytes is modulated by the interaction between the D-serine synthetic enzyme serine racemase (SRR) and a glycolytic enzyme, glyceraldehyde 3-phosphate dehydrogenase (GAPDH). D-serine serine racemase Homo sapiens
3 Here we show that d-serine production in astrocytes is modulated by the interaction between the D-serine synthetic enzyme serine racemase (SRR) and a glycolytic enzyme, glyceraldehyde 3-phosphate dehydrogenase (GAPDH). D-serine serine racemase Homo sapiens
4 Here we show that d-serine production in astrocytes is modulated by the interaction between the D-serine synthetic enzyme serine racemase (SRR) and a glycolytic enzyme, glyceraldehyde 3-phosphate dehydrogenase (GAPDH). D-serine serine racemase Homo sapiens
5 Thus, astrocytic production of D-serine is modulated by glycolytic activity via interactions between GAPDH and SRR. D-serine serine racemase Homo sapiens