Cloned (Comment) | Organism |
---|---|
expression of wild-type and mutant enzyme W84F in Escherichia coli | Geobacillus stearothermophilus |
Protein Variants | Comment | Organism |
---|---|---|
W84F | slightly lower Km-values for NAD+ and glyceraldehyde 3-phosphate, slightly higher Km-value for phosphate. The construction of the mutant permitts the identification of the individual fluorescence and phosphorescence characteristics of the two Trp residues W84 and W310 in the native enzyme | Geobacillus stearothermophilus |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.11 | - |
NAD+ | mutant enzyme W84F | Geobacillus stearothermophilus | |
0.15 | - |
NAD+ | wild-type enzyme | Geobacillus stearothermophilus | |
0.31 | - |
D-glyceraldehyde 3-phosphate | mutant enzyme W48F | Geobacillus stearothermophilus | |
0.8 | - |
D-glyceraldehyde 3-phosphate | wild-type enzyme | Geobacillus stearothermophilus | |
8.3 | - |
phosphate | wild-type enzyme | Geobacillus stearothermophilus | |
9.6 | - |
phosphate | mutant enzyme W84F | Geobacillus stearothermophilus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Geobacillus stearothermophilus | - |
wild-type and mutant W84F | - |
Purification (Comment) | Organism |
---|---|
- |
Geobacillus stearothermophilus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
D-glyceraldehyde 3-phosphate + phosphate + NAD+ | - |
Geobacillus stearothermophilus | 3-phospho-D-glyceroyl phosphate + NADH | - |
? |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
46 | - |
D-glyceraldehyde 3-phosphate | mutant enzyme W84F | Geobacillus stearothermophilus | |
70 | - |
D-glyceraldehyde 3-phosphate | - |
Geobacillus stearothermophilus |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NAD+ | effects of NAD+ binding on the luminescence of Trp84 and Trp310. NAD+-induced conformational change is sequential and subtle rearrangement in the structure of unligated subunits might be responsible for the negative cooperative behavior of NAD+ binding | Geobacillus stearothermophilus |