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Literature summary for 1.2.1.12 extracted from

  • Suzuki, M.; Sasabe, J.; Miyoshi, Y.; Kuwasako, K.; Muto, Y.; Hamase, K.; Matsuoka, M.; Imanishi, N.; Aiso, S.
    Glycolytic flux controls D-serine synthesis through glyceraldehyde-3-phosphate dehydrogenase in astrocytes (2015), Proc. Natl. Acad. Sci. USA, 112, E2217-E2224 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.2.1.12

Protein Variants

Protein Variants Comment Organism
additional information construction of three deletion mutants of GAPDH that lack different lengths in their C-terminal regions (GAPDH1-106, GAPDH1-176, and GAPDH1-230). Among these three mutants, GAPDH1-106 shows an affinity with SRR, whereas GAPDH1-176 and GAPDH1-230 do not, suggesting that the catalytic domain interrupts interacting sites in the NAD+-binding domain of GAPDH Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
D-glyceraldehyde 3-phosphate + phosphate + NAD+ Homo sapiens
-
 3-phospho-D-glyceroyl phosphate + NADH + H+
-
 ?
additional information Homo sapiens the enzyme interacts directly with the D-serine synthetic enzyme serine racemase, SRR. Glyceraldehyde-3-phosphate (G3P) augments the SRR-GAPDH interaction in a dose-dependent manner, whereas NAD+ and its reduced form, NADH, inhibit the interaction ?
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens P04406
-
-

Source Tissue

Source Tissue Comment Organism Textmining
astrocyte primary culture Homo sapiens
-
hippocampus
-
 Homo sapiens
-
additional information astrocytes express SRR in the subiculum of human hippocampal formation Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-glyceraldehyde 3-phosphate + phosphate + NAD+
-
 Homo sapiens 3-phospho-D-glyceroyl phosphate + NADH + H+
-
 ?
additional information the enzyme interacts directly with the D-serine synthetic enzyme serine racemase, SRR. Glyceraldehyde-3-phosphate (G3P) augments the SRR-GAPDH interaction in a dose-dependent manner, whereas NAD+ and its reduced form, NADH, inhibit the interaction Homo sapiens ?
-
 ?

Subunits

Subunits Comment Organism
? x * 37000, SDS-PAGE Homo sapiens
More GAPDH is composed of two folding domains, an NAD+-binding domain (residues 2-150) and a catalytic domain (residues 155-312) Homo sapiens

Synonyms

Synonyms Comment Organism
GAPDH
-
 Homo sapiens
glyceraldehyde 3-phosphate dehydrogenase
-
 Homo sapiens

Cofactor

Cofactor Comment Organism Structure
NAD+ the NAD+-binding domain comprises residues 2-150 Homo sapiens

General Information

General Information Comment Organism
metabolism GAPDH not only catalyses the sixth step of glycolysis, but is also implicated in multiple nonmetabolic processes. Glycolytic flux controls D-serine synthesis through glyceraldehyde-3-phosphate dehydrogenase in astrocytes. Astrocytic energy metabolism controls D-serine production, thereby influencing glutamatergic neurotransmission in the hippocampus, overview. Involvement of glycolysis in modulating D-serine levels Homo sapiens
additional information the enzyme's catalytic domain interrupts interacting sites in the NAD+-binding domain of GAPDH Homo sapiens
physiological function glycolytic flux controls D-serine synthesis through glyceraldehyde-3-phosphate dehydrogenase in astrocytes. 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). In primary cultured astrocytes, glycolysis activity is negatively correlated with D-serine level. SRR interacts directly with GAPDH, and activation of glycolysis augments this interaction. GAPDH suppresses SRR activity by direct binding to GAPDH and through NADH, a product of GAPDH. NADH allosterically inhibits the activity of SRR by promoting the disassociation of ATP from SRR Homo sapiens