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Literature summary for 1.14.16.1 extracted from
- Iron binding effects on the kinetic stability and unfolding energetics of a thermophilic phenylalanine hydroxylase from Chloroflexus aurantiacus (2009), J. Biol. Inorg. Chem., 14, 521-531.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expressed in Escherichia coli BL21(DE3) cells | Chloroflexus aurantiacus |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| additional information | the treatment with EDTA leads to the fully reversible release of iron from the active site without irreversibly inactivating the enzyme | Chloroflexus aurantiacus |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Fe2+ | incubation of apo-PAH with 0.5 mM Fe2+ and removal of free Fe2+ provides a holoenzyme which retains almost stoichiometric amounts of Fe2+ bound (0.88 mol Fe2+/mol monomer) | Chloroflexus aurantiacus |  |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 32000 | 34000 | holo- and apo-enzyme forms display a similar hydrodynamic volume of 32000-34000 Da, apparent molecular mass based on gel filtration | Chloroflexus aurantiacus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Chloroflexus aurantiacus | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| TALON Superflow metal affinity resin column chromatography and Superdex 200 gel filtration | Chloroflexus aurantiacus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| L-phenylalanine + 5,6,7,8-tetrahydrobiopterin + O2 | - |
Chloroflexus aurantiacus | L-tyrosine + 4a-hydroxytetrahydrobiopterin | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| PAH | - |
Chloroflexus aurantiacus |
| phenylalanine hydroxylase | - |
Chloroflexus aurantiacus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 55 | - |
- |
Chloroflexus aurantiacus |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 20 | 60 | holo-phenylalanine hydroxylase displays a large increase in thermal stability (approximately 15°C upshift in the Tm value) compared with the apoenzyme (melting temperature at 64°C), holo-caPAH shows higher kinetic stability at optimal growth temperature (denaturing approximately 8 times more slowly than the apo form at 55°C) | Chloroflexus aurantiacus |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| 5,6,7,8-tetrahydro-L-biopterin | - |
Chloroflexus aurantiacus | |
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