Application | Comment | Organism |
---|---|---|
drug development | the conformation of FgGAPDH in this region is similar to the human enzyme. Therefore, GAPDH may not be a suitable target for drug discovery against fascioliasis caused by Fasciola gigantica | Fasciola gigantica |
Cloned (Comment) | Organism |
---|---|
gene gapdh, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, recombinant expression of His-tagged enzyme in Escherichia coli strain DH5alpha | Fasciola gigantica |
General Stability | Organism |
---|---|
higher salt (300 mM NaCl) concentrations stabilizes the tetrameric state. Also binding of the cofactor NAD+ causes a conformational rearrangement in the enzyme structure, leading to the stabilization of the enzyme | Fasciola gigantica |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | Michaelis-Menten kinetics | Fasciola gigantica | |
0.612 | - |
NAD+ | pH 7.4, 37°C, recombinant enzyme | Fasciola gigantica | |
1.44 | - |
D-glyceraldehyde 3-phosphate | pH 7.4, 37°C, recombinant enzyme | Fasciola gigantica |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
145000 | - |
recombinant His-tagged enzyme, gel filtration | Fasciola gigantica |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
D-glyceraldehyde 3-phosphate + phosphate + NAD+ | Fasciola gigantica | - |
3-phospho-D-glyceroyl phosphate + NADH + H+ | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Fasciola gigantica | A0A504YZJ3 | - |
- |
Purification (Comment) | Organism |
---|---|
recombinant His-tagged enzyme from Escherichia coli strain DH5alpha by nickel affinity chromatography and dialysis, to homogeneity | Fasciola gigantica |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
D-glyceraldehyde 3-phosphate + phosphate + NAD+ | - |
Fasciola gigantica | 3-phospho-D-glyceroyl phosphate + NADH + H+ | - |
? | |
additional information | substrate and cofactor binding analysis and kinetics, overview | Fasciola gigantica | ? | - |
- |
Subunits | Comment | Organism |
---|---|---|
homotetramer | 4 * 37000, recombinant His-tagged enzyme, SDS-PAGE | Fasciola gigantica |
Synonyms | Comment | Organism |
---|---|---|
FgGAPDH | - |
Fasciola gigantica |
GAPDH | - |
Fasciola gigantica |
glyceraldehyde 3-phosphate dehydrogenase | - |
Fasciola gigantica |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Fasciola gigantica |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
1.43 | - |
NAD+ | pH 7.4, 37°C, recombinant enzyme | Fasciola gigantica | |
1.58 | - |
D-glyceraldehyde 3-phosphate | pH 7.4, 37°C, recombinant enzyme | Fasciola gigantica |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.4 | - |
assay at | Fasciola gigantica |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NAD+ | binding of NAD+ cofactor causes a conformational rearrangement in the enzyme structure, leading to the stabilization of the enzyme | Fasciola gigantica |
Organism | Comment | pI Value Maximum | pI Value |
---|---|---|---|
Fasciola gigantica | sequence calculation | - |
7.1 |
General Information | Comment | Organism |
---|---|---|
metabolism | glyceraldehyde 3-phosphate dehydrogenase (FgGAPDH) is a key enzyme of the glycolytic pathway | Fasciola gigantica |
additional information | docking analysis of cofactor NAD+ and substrate glyceraldehyde 3-phosphate, identification and structure analysis of the binding sites, overview. Enzyme structure homology modeling using the structure of NAD+ bound BmGAPDH from Brugia malayi (PDB ID 4K9D) as template | Fasciola gigantica |
physiological function | in Fasciola gigantica, the glyceraldehyde 3-phosphate dehydrogenase (FgGAPDH) is a key enzyme of the glycolytic pathway and catalyzes the reversible oxidative phosphorylation of D-glyceraldehyde-3-phosphate to 1,3-bisphosphoglycerate, with the simultaneous reduction of NAD+ to NADH. The enzyme has various roles in the parasite | Fasciola gigantica |
kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
1.097 | - |
D-glyceraldehyde 3-phosphate | pH 7.4, 37°C, recombinant enzyme | Fasciola gigantica | |
2.337 | - |
NAD+ | pH 7.4, 37°C, recombinant enzyme | Fasciola gigantica |