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Literature summary for 1.14.16.1 extracted from

  • Kappock, T.J.; Harkins, P.C.; Friedenberg, S.; Caradonna, J.P.
    Spectroscopic and kinetic properties of unphosphorylated rat hepatic phenylalanine hydroxylase expressed in Escherichia coli. Comparison of resting and activated states (1995), J. Biol. Chem., 270, 30532-30544.
    View publication on PubMed
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Activating Compound

Activating Compound Comment Organism Structure
phenylalanine homotropic allosteric activator of both hepatic and recombinant enzymes Rattus norvegicus

Cloned(Commentary)

Cloned (Comment) Organism
-
 Rattus norvegicus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.045
-
 6-methyltetrahydropterin
-
 Rattus norvegicus
0.061
-
 6-methyltetrahydropterin recombinant enzyme Rattus norvegicus
0.17
-
 phenylalanine cofactor 6-methyltetrahydropterin, recombinant enzyme Rattus norvegicus
0.18
-
 phenylalanine cofactor 6-methyltetrahydropterin Rattus norvegicus

Metals/Ions

Metals/Ions Comment Organism Structure
Iron maximal 1 iron per subunit, hepatic and recombinant enzyme Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
side-chain modification recombinant enzyme incorporates 0.97 phosphate per subunit Rattus norvegicus

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme Rattus norvegicus

Source Tissue

Source Tissue Comment Organism Textmining

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
6.8
-
 recombinant enzyme Rattus norvegicus