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Literature summary for 1.14.16.1 extracted from

  • Dobrowolski, S.F.; Pey, A.L.; Koch, R.; Levy, H.; Ellingson, C.C.; Naylor, E.W.; Martinez, A.
    Biochemical characterization of mutant phenylalanine hydroxylase enzymes and correlation with clinical presentation in hyperphenylalaninaemic patients (2009), J. Inherit. Metab. Dis., 32, 10-21.
    View publication on PubMed
Search for more literature for 1.14.16.1

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli as fusion proteins with maltose-binding protein Homo sapiens

Protein Variants

Protein Variants Comment Organism
D143G mutant with a mild misfolding defect associated with phenylketonuria Homo sapiens
L348V the mutant retains significant catalytic activity yet is observed in classic and moderate phenylketonuria patients Homo sapiens
P416Q the mutant retains significant catalytic activity yet is observed in classic and moderate phenylketonuria patients Homo sapiens
R155H the mutant displays low PAH activity and decreased apparent affinity for L-Phe yet is observed in mild hyperphenylalaninaemia, mutant does not display kinetic instability, as it is stabilized by (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin similarly to wild type enzyme Homo sapiens
R408W the mutant is dysfunctional in nearly all biochemical parameters, as evidenced by disease severity in homozygous and hemizygous patients Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.027
-
 (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin mutant enzyme R155H, in 100 mM Na-HEPES buffer, pH 7.0, at 25°C Homo sapiens
0.03
-
 (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin mutant enzyme P416Q, in 100 mM Na-HEPES buffer, pH 7.0, at 25°C Homo sapiens
0.033
-
 (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin wild type enzyme, in 100 mM Na-HEPES buffer, pH 7.0, at 25°C Homo sapiens
0.035
-
 (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin mutant enzyme R408W, in 100 mM Na-HEPES buffer, pH 7.0, at 25°C Homo sapiens
0.04
-
 (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin mutant enzyme L348V, in 100 mM Na-HEPES buffer, pH 7.0, at 25°C Homo sapiens
0.053
-
 (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin mutant enzyme D143G, in 100 mM Na-HEPES buffer, pH 7.0, at 25°C Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens P00439
-
-

Purification (Commentary)

Purification (Comment) Organism
Superdex 200 gel filtration Homo sapiens

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.75
-
 mutant enzyme R408W, using L-phenylalanine as substrate, in 100 mM Na-HEPES buffer, pH 7.0, at 25°C Homo sapiens
1.32
-
 mutant enzyme R155H, using L-phenylalanine as substrate, in 100 mM Na-HEPES buffer, pH 7.0, at 25°C Homo sapiens
1.64
-
 mutant enzyme D143G, using L-phenylalanine as substrate, in 100 mM Na-HEPES buffer, pH 7.0, at 25°C Homo sapiens
2.76
-
 mutant enzyme L348V, using L-phenylalanine as substrate, in 100 mM Na-HEPES buffer, pH 7.0, at 25°C Homo sapiens
2.98
-
 wild type enzyme, using L-phenylalanine as substrate, in 100 mM Na-HEPES buffer, pH 7.0, at 25°C Homo sapiens
3.32
-
 mutant enzyme P416Q, using L-phenylalanine as substrate, in 100 mM Na-HEPES buffer, pH 7.0, at 25°C Homo sapiens

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
tetramer
-
 Homo sapiens

Synonyms

Synonyms Comment Organism
PAH
-
 Homo sapiens
phenylalanine hydroxylase
-
 Homo sapiens

Cofactor

Cofactor Comment Organism Structure
(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin
-
 Homo sapiens

General Information

General Information Comment Organism
malfunction phenylketonuria results from defects in phenylalanine hydroxylase Homo sapiens