Literature summary for 1.14.16.1 extracted from

Bjorgo, E.; De Carvalho, R.M.N.; Flatmark, T.
A comparison of kinetic and regulatory properties of the tetrameric and dimeric forms of wild-type and Thr427->Pro mutant human phenylalanine hydroxylase. Contribution of the flexible hinge region Asp425-Gln429 to the tetramerization and cooperative substrate binding (2001), Eur. J. Biochem., 268, 997-1005.

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Activating Compound

Activating Compound	Comment	Organism	Structure
phenylalanine	-	Rattus norvegicus
phenylalanine	after activation with phenylalanine the dimer/tetramer equilibrium is shifted towards the tetrameric form	Homo sapiens
phenylalanine	wild-type tetramer reveals a kinetic positive coorperativity of L-phenylalanine binding leading to a 5-6fold activation of wild-type tetramer, dimeric form shows a hyperbolic rate vs. substrate concentration, 1.6fold activation by phenylalanine, tetrameric T427P mutant enzyme shows no cooperativity, dimeric forms of wild-type and T427P mutant have similar kinetic properties	Homo sapiens

Cloned(Commentary)

Cloned (Comment)	Organism
expression of wild-type and T427P mutant enzyme in Escherichia coli	Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
T427P	increase in the amount of oligomeric forms higher than tetramers after preincubation of a mixture of dimeric and tetrameric forms with phenylalanine, tetrameric form exhibits approx. 50% of wild-type tetramer phenylalanine hydroxylase activity	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-
Rattus norvegicus	-	-	-

Subunits

Subunits	Comment	Organism
More	rat liver enzyme and recombinant human enzyme are in a tetramer/dimer equilibrium	Homo sapiens
More	rat liver enzyme and recombinant human enzyme are in a tetramer/dimer equilibrium	Rattus norvegicus

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Release 2023.1 (January 2023)