Activating Compound | Comment | Organism | Structure |
---|---|---|---|
phenylalanine | - |
Rattus norvegicus | |
phenylalanine | after activation with phenylalanine the dimer/tetramer equilibrium is shifted towards the tetrameric form | Homo sapiens | |
phenylalanine | wild-type tetramer reveals a kinetic positive coorperativity of L-phenylalanine binding leading to a 5-6fold activation of wild-type tetramer, dimeric form shows a hyperbolic rate vs. substrate concentration, 1.6fold activation by phenylalanine, tetrameric T427P mutant enzyme shows no cooperativity, dimeric forms of wild-type and T427P mutant have similar kinetic properties | Homo sapiens |
Cloned (Comment) | Organism |
---|---|
expression of wild-type and T427P mutant enzyme in Escherichia coli | Homo sapiens |
Protein Variants | Comment | Organism |
---|---|---|
T427P | increase in the amount of oligomeric forms higher than tetramers after preincubation of a mixture of dimeric and tetrameric forms with phenylalanine, tetrameric form exhibits approx. 50% of wild-type tetramer phenylalanine hydroxylase activity | Homo sapiens |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
- |
- |
Rattus norvegicus | - |
- |
- |
Subunits | Comment | Organism |
---|---|---|
More | rat liver enzyme and recombinant human enzyme are in a tetramer/dimer equilibrium | Homo sapiens |
More | rat liver enzyme and recombinant human enzyme are in a tetramer/dimer equilibrium | Rattus norvegicus |