Cloned (Comment) | Organism |
---|---|
- |
Corynebacterium callunae |
Protein Variants | Comment | Organism |
---|---|---|
R226A | site-directed mutagenesis, mutant enzyme shows 4fold increased inactivation rate during subunit dissociation at 30°C in absence of an oxyanion, but similar stability in presence of 5 mM sulfate or phosphate compared to the wild-type enzyme | Corynebacterium callunae |
R234A | site-directed mutagenesis, mutant enzyme shows 4fold reduced inactivation rate during subunit dissociation at 30°C in absence of an oxyanion, but reduced stability in presence of 5 mM sulfate or phosphate compared to the wild-type enzyme, 8fold reduced affinity for phosphate | Corynebacterium callunae |
R242A | site-directed mutagenesis, mutant enzyme shows 4fold reduced inactivation rate during subunit dissociation at 30°C in absence of an oxyanion, but reduced stability in presence of 5 mM phosphate compared to the wild-type enzyme, 20fold reduced affinity for phosphate | Corynebacterium callunae |
S224A | site-directed mutagenesis, mutant enzyme shows 4fold increased inactivation rate during subunit dissociation at 30°C in absence of an oxyanion, but similar stability in presence of 5 mM sulfate or phosphate compared to the wild-type enzyme | Corynebacterium callunae |
S238A | site-directed mutagenesis, mutant enzyme shows 4fold increased inactivation rate during subunit dissociation at 30°C in absence of an oxyanion, but similar stability in presence of 5 mM sulfate or phosphate compared to the wild-type enzyme | Corynebacterium callunae |
General Stability | Organism |
---|---|
half-lives of wild-type and mutant enzymes under dissociation/inactivation conditions at 30°C and pH 7.0 in 0.4 M imidazole citrate buffer, pH 7.5, and 0.1 mM L-cysteine, overview | Corynebacterium callunae |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
additional information | maltohexaose causes negligible substrate inhibition with Ki of 360 mM | Corynebacterium callunae |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
2.65 | - |
maltohexaose | recombinant wild-type enzyme | Corynebacterium callunae | |
6 | - |
phosphate | recombinant wild-type enzyme | Corynebacterium callunae |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Corynebacterium callunae | - |
- |
- |
Renatured (Comment) | Organism |
---|---|
reconstitution of wild-type and mutant apoenzymes with cofactor pyridoxal 5'-phosphate, the rate of regained activity is increased up to 4.5fold by addition of phosphate, recovery of 60% and 5% wild-type activity at 3 mM and 5 mM, rate of recovery with mutant enzymes, respectively, pyridoxal does not recover the activity, rate of recovery with mutant enzymes, overview | Corynebacterium callunae |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
maltohexaose + alpha-D-glucose 1-phosphate | - |
Corynebacterium callunae | maltoheptaose + phosphate | - |
r |
Subunits | Comment | Organism |
---|---|---|
dimer | homodimer, can be reversibly dissociated at 30°C in 0.4 M imidazole citrate buffer, pH 7.5, and 0.1 mM L-cysteine into native-like folded subunits with release of cofactor pyridoxal 5'-phosphate and loss of activity, phosphate and sulfate protect against inactivation via dissociation, overview | Corynebacterium callunae |
More | an enzyme subunit does not form hybrid dimers with a subunit of Escherichia coli maltodextrin phosphorylase | Corynebacterium callunae |
Synonyms | Comment | Organism |
---|---|---|
starch phosphorylase | - |
Corynebacterium callunae |
StP | - |
Corynebacterium callunae |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
assay at | Corynebacterium callunae |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
50 | - |
pH 7.0, in presence of pyridoxal 5'-phosphate, stable | Corynebacterium callunae |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7 | - |
assay at | Corynebacterium callunae |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
5 | 8 | - |
Corynebacterium callunae |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
pyridoxal 5'-phosphate | dependent on, reversible dissociation study | Corynebacterium callunae |