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Literature summary for 1.14.16.1 extracted from

  • Shiman, R.; Gray, D.W.; Hill, M.A.
    Regulation of rat liver phenylalanine hydroxylase. I. Kinetic properties of the enzyme's iron and enzyme reduction site (1994), J. Biol. Chem., 269, 24637-24646.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
2,3-dihydroxynaphthalene binds to Fe3+ on enzyme that is oxidized during catalysis Rattus norvegicus
Acetohydroxamate competitive vs. tetrahydrobiopterin, most probably due to chelation of enzyme's iron Rattus norvegicus
bathophenanthroline competitive vs. 6-methyl-5,6,7,8-tetrahydropterin and tetrahydrobiopterin, most probably due to chelation of enzyme's iron Rattus norvegicus
benzohydroxamate competitive vs. tetrahydrobiopterin, most probably due to chelation of enzyme's iron Rattus norvegicus
o-phenanthroline 1 mM, removes Fe2+ from the reduced enzyme Rattus norvegicus

Metals/Ions

Metals/Ions Comment Organism Structure
Iron kinetic data suggest, that enzyme's iron is solvent-accessible and resides in a hydrophobic pocket of the enzyme Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.0000015
-
bathophenanthroline vs. tetrahydrobiopterin Rattus norvegicus
0.0000018
-
bathophenanthroline vs. 6-methyl-5,6,7,8-tetrahydropterin Rattus norvegicus
0.07
-
benzohydroxamate
-
Rattus norvegicus
1.7
-
Acetohydroxamate
-
Rattus norvegicus