Application | Comment | Organism |
---|---|---|
drug development | development of GAPDH inhibitors as anti-cancer and anti-parasitic agents | Fasciola hepatica |
Cloned (Comment) | Organism |
---|---|
FhGAPDH sequence comparisons, functional recombinant expression of His-tagged enzyme in Escherichia coli strain Rosetta(DE3) | Fasciola hepatica |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
additional information | development of GAPDH inhibitors as anti-cancer and anti-parasitic agents | Fasciola hepatica |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | the recombinant protein shows no cooperativity towards glyceraldehyde 3-phosphate as a substrate, Michaelis-Menten kinetics with glyceraldehyde 3-phosphate as a substrate | Fasciola hepatica |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
113000 | - |
recombinant enzyme, gel filtration | Fasciola hepatica |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
D-glyceraldehyde 3-phosphate + phosphate + NAD+ | Fasciola hepatica | - |
3-phospho-D-glyceroyl phosphate + NADH + H+ | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Fasciola hepatica | A0A068LJN3 | - |
- |
Purification (Comment) | Organism |
---|---|
recombinant His-tagged enzyme from Escherichia coli strain Rosetta(DE3) by nickel affinity chromatography | Fasciola hepatica |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
D-glyceraldehyde 3-phosphate + phosphate + NAD+ | - |
Fasciola hepatica | 3-phospho-D-glyceroyl phosphate + NADH + H+ | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer | 2 * 37000, about, sequence calculation, ligands bound | Fasciola hepatica |
More | purified recombinant FhGAPDH is a mixture of homodimers and tetramers, as judged by protein-protein crosslinking and analytical gel filtration. The addition of either NAD+ or glyceraldehyde 3-phosphate shifts this equilibrium towards a compact dimer, that is more stable than the unliganded one. Molecular modeling of FhGAPDH monomer, and of the enzyme as a tetramer, the quaternary structure is shown as a dimer of dimers arrangement, overview. Substrate binding induces conformational and oligomerisation changes in FhGAPDH, both glyceraldehyde 3-phosphate and NAD+ appear to favour the formation of dimers over tetramers | Fasciola hepatica |
tetramer | 4 * 37000, about, sequence calculation and modeling | Fasciola hepatica |
Synonyms | Comment | Organism |
---|---|---|
FhGAPDH | - |
Fasciola hepatica |
GAPDH | - |
Fasciola hepatica |
glyceraldehyde 3-phosphate dehydrogenase | - |
Fasciola hepatica |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at, NAD+ reduction | Fasciola hepatica |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
additional information | - |
the addition of either NAD+ or glyceraldehyde 3-phosphate shifts this equilibrium towards a compact dimer, that is more stable than the unliganded one, thermal scanning fluorimetry | Fasciola hepatica |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.6 | - |
assay at, NAD+ reduction | Fasciola hepatica |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NAD+ | - |
Fasciola hepatica | |
NADH | - |
Fasciola hepatica |
Organism | Comment | pI Value Maximum | pI Value |
---|---|---|---|
Fasciola hepatica | sequence calculation | - |
7.1 |
General Information | Comment | Organism |
---|---|---|
malfunction | inhibition of GAPDH leads to substantially reduced energy generation | Fasciola hepatica |
additional information | molecular modeling of FhGAPDH monomer, overview. Substrate binding induces conformational and oligomerisation changes in FhGAPDH, both glyceraldehyde 3-phosphate and NAD+ appear to favour the formation of dimers over tetramers | Fasciola hepatica |
physiological function | glyceraldehyde 3-phosphate dehydrogenase (GAPDH) catalyses one of the two steps in glycolysis which generate the reduced coenzyme NADH. This reaction precedes the two ATP generating steps | Fasciola hepatica |