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Literature summary for 2.4.1.1 extracted from
- Relationships between structure, function and stability for pyridoxal 5'-phosphate-dependent starch phosphorylase from Corynebacterium callunae as revealed by reversible cofactor dissociation studies (2004), Eur. J. Biochem., 271, 3319-3329.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
- |
Corynebacterium callunae |
Protein Variants
| 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
| 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
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| additional information | maltohexaose causes negligible substrate inhibition with Ki of 360 mM | Corynebacterium callunae |
KM Value [mM]
| 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
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Corynebacterium callunae | - |
- |
- |
Renatured (Commentary)
| 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 and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| maltohexaose + alpha-D-glucose 1-phosphate | - |
Corynebacterium callunae | maltoheptaose + phosphate | - |
r | |
Subunits
| 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
| Synonyms | Comment | Organism |
|---|---|---|
| starch phosphorylase | - |
Corynebacterium callunae |
| StP | - |
Corynebacterium callunae |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | - |
assay at | Corynebacterium callunae |
Temperature Stability [°C]
| 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
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7 | - |
assay at | Corynebacterium callunae |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 5 | 8 | - |
Corynebacterium callunae |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| pyridoxal 5'-phosphate | dependent on, reversible dissociation study | Corynebacterium callunae | |
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