Cloned (Comment) | Organism |
---|---|
regulatory domain (amino acids 1-118) of rat phenylalanine hydroxylase is expressed in Escherichia coli | Rattus norvegicus |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
13000 | - |
2 * 13000 (regulatory domain 1-118), gel filtration. In the presence of phenylalanine, the protein elutes earlier from the column, consistent with a conformational change in the presence of the amino acid | Rattus norvegicus |
26000 | - |
gel filtration, regulatory domain (amino acids 1-118) | Rattus norvegicus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Rattus norvegicus | - |
- |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
L-phenylalanine + a 5,6,7,8-tetrahydropteridine + O2 = L-tyrosine + a 4a-hydroxy-5,6,7,8-tetrahydropteridine | 1H-15N HSQC NMR spectra are obtained of the 15N-labeled protein alone and in the presence of phenylalanine. Regulatory domain of phenylalanine hydroxylase can bind phenylalanine, consistent with the presence of an allosteric site for the amino acid | Rattus norvegicus |
Subunits | Comment | Organism |
---|---|---|
dimer | 2 * 13000 (regulatory domain 1-118), gel filtration. In the presence of phenylalanine, the protein elutes earlier from the column, consistent with a conformational change in the presence of the amino acid | Rattus norvegicus |
Synonyms | Comment | Organism |
---|---|---|
phenylalanine hydroxylase | - |
Rattus norvegicus |