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Literature summary for 1.14.16.1 extracted from

  • Chen, D.; Frey, P.A.
    Phenylalanine hydroxylase from Chromobacterium violaceum. Uncoupled oxidation of tetrahydropterin and the role of iron in hydroxylation (1998), J. Biol. Chem., 273, 25594-25601.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Chromobacterium violaceum

Metals/Ions

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 [Da] Molecular Weight Maximum [Da] Comment Organism
33613
-
1 * 33613, deduced from nucleotide sequence Chromobacterium violaceum

Organism

Organism UniProt Comment Textmining
Chromobacterium violaceum
-
most probably 2 phenylalanine hydroxylases encoded by different genes
-

Substrates and Products (Substrate)

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

Subunits Comment Organism
monomer 1 * 33483-33488, recombinant enzyme, mass spectrometry Chromobacterium violaceum
monomer 1 * 33613, deduced from nucleotide sequence Chromobacterium violaceum