Literature summary for 1.14.16.1 extracted from

Flydal, M.I.; Mohn, T.C.; Pey, A.L.; Siltberg-Liberles, J.; Teigen, K.; Martinez, A.
Superstoichiometric binding of L-Phe to phenylalanine hydroxylase from Caenorhabditis elegans: evolutionary implications (2010), Amino Acids, 39, 1463-1475.

Search for more literature for 1.14.16.1

Cloned(Commentary)

Cloned (Comment)	Organism
expressed in Escherichia coli	Caenorhabditis elegans

Protein Variants

Protein Variants	Comment	Organism
Q215K/N216Y	humanized mutant Q215K/N216Y of cePAH binds 1.4 L-Phe/subunit. This mutant also displays high catalytic activity and certain positive cooperativity for L-Phe. Km for cofactor tetrahydrobiopterin higher compared to wild-type, [S]0.5 (L-Phe) lower compared to wild-type, Vmax (L-Phe) higher compared to wild-type	Caenorhabditis elegans

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
additional information	-	additional information	[S]0.5 (L-phenylalanine): 0.188 mM wild-type,0,109 mM mutant Q215K/N216Y, Vmax (wild-type): 1.9 micromol L-Tyr/min/mg, Vmax (mutant Q215K/N216Y): 6.6 micromol L-Tyr/min/mg, pH 7.0, 25°C	Caenorhabditis elegans
0.029	-	(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin	wild-type, pH 7.0, 25°C	Caenorhabditis elegans
0.094	-	(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin	mutant Q215K/N216Y, pH 7.0, 25°C	Caenorhabditis elegans

Organism

Organism	UniProt	Comment	Textmining
Caenorhabditis elegans	-	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
L-phenylalanine + a 5,6,7,8-tetrahydropteridine + O2 = L-tyrosine + a 4a-hydroxy-5,6,7,8-tetrahydropteridine	structural analysis reveal an additional L-Phe binding site at the regulatory domain of full-length cePAH. This site involves the GA(S)L/ISRP motifs, which are also found in ACT domains of other L-Phe binding proteins	Caenorhabditis elegans	a

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
2.1	-	micromol L-Tyr/min/mg, wild-type, pH 7.0, 25°C, without L-Phe preincubated enzyme	Caenorhabditis elegans
2.6	-	micromol L-Tyr/min/mg, wild-type, pH 7.0, 25°C, with L-Phe preincubated enzyme	Caenorhabditis elegans
4.9	-	micromol L-Tyr/min/mg, mutant Q215K/N216Y, pH 7.0, 25°C, with L-Phe preincubated enzyme	Caenorhabditis elegans
6.5	-	micromol L-Tyr/min/mg, mutant Q215K/N216Y, pH 7.0, 25°C, with L-Phe preincubated enzyme	Caenorhabditis elegans

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
L-phenylalanine + (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin + O2	-	Caenorhabditis elegans	L-tyrosine + 4a-hydroxy-(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin	-	?

Subunits

Subunits	Comment	Organism
tetramer	-	Caenorhabditis elegans

Synonyms

Synonyms	Comment	Organism
cePAH	-	Caenorhabditis elegans
phenylalanine hydroxylase	-	Caenorhabditis elegans

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
25	-	assay at	Caenorhabditis elegans

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7	-	assay at	Caenorhabditis elegans

Cofactor

Cofactor	Comment	Organism	Structure
tetrahydrobiopterin	-	Caenorhabditis elegans

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Release 2023.1 (January 2023)