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Literature summary for 1.2.1.12 extracted from

  • Zhang, K.; Sun, W.; Huang, L.; Zhu, K.; Pei, F.; Zhu, L.; Wang, Q.; Lu, Y.; Zhang, H.; Jin, H.; Zhang, L.H.; Zhang, L.; Yue, J.
    Identifying glyceraldehyde 3-phosphate dehydrogenase as a cyclic adenosine diphosphoribose binding protein by photoaffinity protein-ligand labeling approach (2017), J. Am. Chem. Soc., 139, 156-170 .
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
D234A site-directed mutagenesis Homo sapiens
H179A site-directed mutagenesis, the KD value of cADPR to GAPDHHis179Ala mutant protein is markedly increased compared to wild-type GAPDH enzyme 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
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3-phospho-D-glyceroyl phosphate + NADH + H+
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?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
coronary artery smooth muscle cell
-
Homo sapiens
-
HEK-293 cell
-
Homo sapiens
-
JURKAT cell
-
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 GAPDH directly binds to cyclic adenosine diphosphoribose (cADPR), molecule docking and molecular dynamic simulations, overview. Arg234 and His179 in GAPDH might be the potential binding sites for cADPR Homo sapiens ?
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?

Subunits

Subunits Comment Organism
tetramer
-
Homo sapiens

Synonyms

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

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.5
-
assay at Homo sapiens

Cofactor

Cofactor Comment Organism Structure
NAD+
-
Homo sapiens

General Information

General Information Comment Organism
malfunction GAPDH knockdown abolishes cADPR-induced Ca2+ release. GAPDH knockdown markedly inhibits NPE-cADPR- or PALcIDPRE-induced cytosolic Ca2+ increase in Jurkat cells, RyR3-expressing HEK-293 cells, or human coronary artery smooth muscle cells. Washing saponin-treated cells with PBS abolishes cADPR-induced colocalization of GAPDH with ryanodine receptors, RyRs Homo sapiens
physiological function GAPDH plays essential role in glycolysis and gluconeogenesis as a housekeeping enzyme. Cyclic adenosine diphosphoribose (cADPR), an endogenous nucleotide derived from NAD+, mobilizes Ca2+ release from endoplasmic reticulum via ryanodine receptors (RyRs). cADPR interacts directly with enzyme GAPDH and induces the transient interaction between GAPDH and RyRs in vivo, without cADPR the interaction is weak. GAPDH is required for cADPR-mediated Ca2+ mobilization from endoplasmic reticulum via RyRs. cADPR-mediated Ca2+ signaling pathway is involved in a wide variety of cellular processes,1 e.g. abscisic acid signaling, calorie restriction in gut stem cell, circadian clock in plants, and long-term synaptic depression in hippocampus Homo sapiens