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Literature summary for 1.2.1.12 extracted from

  • Nakajima, H.; Amano, W.; Fujita, A.; Fukuhara, A.; Azuma, Y.T.; Hata, F.; Inui, T.; Takeuchi, T.
    The active site cysteine of the proapoptotic protein glyceraldehyde-3-phosphate dehydrogenase is essential in oxidative stress-induced aggregation and cell death (2007), J. Biol. Chem., 282, 26562-26574.
    View publication on PubMed
Search for more literature for 1.2.1.12

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli strain W3CG and in HeLa cells Oryctolagus cuniculus
expressed in Escherichia coli strainW3CG and in HeLa cells Homo sapiens

Protein Variants

Protein Variants Comment Organism
C149S treatment of with (E)-4-ethyl-2-[(E)-hydroxyimino]-5-nitro-3-hexenamide at 0.1 mM leads to low levels of aggregation (5% of wild type) Oryctolagus cuniculus
C149S/C281S mutant shows a complete absence of aggregation in the presence of (E)-4-ethyl-2-[(E)-hydroxyimino]-5-nitro-3-hexenamide Oryctolagus cuniculus
C153S aggregation can be detected at low concentrations of (E)-4-ethyl-2-[(E)-hydroxyimino]-5-nitro-3-hexenamide (0.001 mM) and is enhanced at higher concentrations Oryctolagus cuniculus
C244A aggregation can be detected at low concentrations of (E)-4-ethyl-2-[(E)-hydroxyimino]-5-nitro-3-hexenamide (0.001 mM) and is enhanced at higher concentrations Oryctolagus cuniculus
C281S the levels of aggregation in C281S are reduced to 45% of wild type at 0.1 mM (E)-4-ethyl-2-[(E)-hydroxyimino]-5-nitro-3-hexenamide Oryctolagus cuniculus

Inhibitors

Inhibitors Comment Organism Structure
(E)-4-ethyl-2-[(E)-hydroxyimino]-5-nitro-3-hexenamide treatment with (E)-4-ethyl-2-[(E)-hydroxyimino]-5-nitro-3-hexenamide between 0.001 and 1 mM induces the oligomerization of GAPDH, dithiothreitol reduces (E)-4-ethyl-2-[(E)-hydroxyimino]-5-nitro-3-hexenamide-induced aggregation in a concentration-dependent manner Oryctolagus cuniculus
1-hydroxy-2-oxo-3,3-bis(2-aminoethyl)-1-triazene
-
 Homo sapiens
1-hydroxy-2-oxo-3,3-bis(2-aminoethyl)-1-triazene
-
 Oryctolagus cuniculus
H2O2
-
 Homo sapiens
H2O2
-
 Oryctolagus cuniculus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
36000
-
 SDS-PAGE, native enzyme Oryctolagus cuniculus
36000
-
 SDS-PAGE, native enzyme Homo sapiens
70000
-
 SDS-PAGE, treatment of GAPDH with (E)-4-ethyl-2-[(E)-hydroxyimino]-5-nitro-3-hexenamide at 0.01 mM for 10 min at 37°C results in formation of three bands (66, 68, and 76 kDa) corresponding roughly to a dimer of 70000 Da Oryctolagus cuniculus

Organism

Organism UniProt Comment Textmining
Homo sapiens P04406
-
-
Oryctolagus cuniculus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
Ni-NTA agarose resin chromatography and Hi-Load 16/60 Superdex gel filtration Oryctolagus cuniculus
Ni-NTA agarose resin chromatography and Hi-Load 16/60 Superdex gel filtration Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining
muscle
-
 Oryctolagus cuniculus
-
neuroblastoma cell
-
 Homo sapiens
-
SH-SY5Y cell
-
 Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-glyceraldehyde 3-phosphate + phosphate + NAD+
-
 Oryctolagus cuniculus 3-phospho-D-glyceroyl phosphate + NADH + H+
-
 ?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
-
 Homo sapiens 3-phospho-D-glyceroyl phosphate + NADH + H+
-
 ?

Subunits

Subunits Comment Organism
monomer 1 * 36000, SDS-PAGE Oryctolagus cuniculus
monomer 1 * 36000, SDS-PAGE Homo sapiens

Synonyms

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

Cofactor

Cofactor Comment Organism Structure
NAD+
-
 Oryctolagus cuniculus
NAD+
-
 Homo sapiens