Literature summary for 1.2.1.12 extracted from

Arutyunova, E.I.; Domnina, L.V.; Chudinova, A.A.; Makshakova, O.N.; Arutyunov, D.Y.; Muronetz, V.I.
Localization of non-native D-glyceraldehyde-3-phosphate dehydrogenase in growing and apoptotic HeLa cells (2013), Biochemistry (Moscow), 78, 91-95 .

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Activating Compound

Activating Compound	Comment	Organism	Structure
actin	GAPDH catalytic activity is increased upon association with actin	Homo sapiens

Inhibitors

Inhibitors	Comment	Organism	Structure
tubulin	GAPDH catalytic activity is inhibited upon formation of a complex with tubulin	Homo sapiens

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
actin filament	specific interaction of actin with non-native GAPDH, i.e. dimers, monomers, the denatured forms of GAPDH	Homo sapiens	5884	-
cytoplasm	predominantly cytoplasmic localization of tetrameric native form GAPDH within HeLa cells	Homo sapiens	5737	-
additional information	immunohistochemic analysis of subcellular enzyme localization	Homo sapiens	-	-
nucleus	non-native GAPDH is unevenly distributed within the nuclei	Homo sapiens	5634	-

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+	-	r

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
HeLa cell	expressing Bcl-2, overproduction of the Bcl-2 protein does not change the non-native GAPDH localization in the growing HeLa-Bcl-2 cells	Homo sapiens	-
HeLa cell	staining of HeLa cells with mAbs 6C5 reveals the predominant accumulation of the non-native forms of GAPDH, i.e. dimers, monomers, the denatured forms of GAPDH, in the nucleus during normal growth	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+	-	r

Subunits

Subunits	Comment	Organism
tetramer	-	Homo sapiens

Synonyms

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

Cofactor

Cofactor	Comment	Organism	Structure
NAD+	-	Homo sapiens
NADH	-	Homo sapiens

General Information

General Information	Comment	Organism
additional information	possible existence of actin/active GAPDH dimer complexes similar to 3-phosphoglycerate kinase/active GAPDH dimer complexes	Homo sapiens
physiological function	the significance of D-glyceraldehyde-3-phosphate dehydrogenase is not restricted to its pivotal glycolytic function. GAPDH localized in the nucleus can be involved in numerous processes: regulation of the length of telomeres, DNA repair, gene expression, and regulation of cyclin functions. GAPDH may act as a specific scaffold for cytoskeleton-associated proteins independently of its catalytic activity	Homo sapiens

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Release 2023.1 (January 2023)