Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli | Chromobacterium violaceum |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Ca2+ | substoichiometric amounts after removal of copper with dithiothreitol | Chromobacterium violaceum | |
copper | copper does not support enzyme activity and can be removed by dithiothreitol | Chromobacterium violaceum | |
Iron | copper depleted enzyme can be reconstituted with approx. 1 molecule of iron per enzyme molecule, iron reconstituted enzyme hydroxylates phenylalanine | Chromobacterium violaceum | |
Zn2+ | substoichiometric amounts after removal of copper with dithiothreitol | Chromobacterium violaceum |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
33613 | - |
1 * 33613, deduced from nucleotide sequence | Chromobacterium violaceum |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Chromobacterium violaceum | - |
most probably 2 phenylalanine hydroxylases encoded by different genes | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-phenylalanine + 6-methyltetrahydropterin + O2 | - |
Chromobacterium violaceum | L-tyrosine + 4a-hydroxy-6-methyltetrahydropterin | in the presence of FeSO4 and dithiothreitol | ? | |
L-phenylalanine + 6-methyltetrahydropterin + O2 | copper-depleted enzyme, in the absence of Fe2+, 6-methyltetrahydropterin oxidation can be uncoupled from substrate hydroxylation by the exclusion of iron | Chromobacterium violaceum | L-tyrosine + 4a-hydroxy-6-methyltetrahydropterin | - |
? |
Subunits | Comment | Organism |
---|---|---|
monomer | 1 * 33483-33488, recombinant enzyme, mass spectrometry | Chromobacterium violaceum |
monomer | 1 * 33613, deduced from nucleotide sequence | Chromobacterium violaceum |