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Literature summary for 1.14.16.1 extracted from

  • Steventon, G.B.; Mitchell, S.C.
    Phenylalanine 4-monooxygenase and the role of endobiotic metabolism enzymes in xenobiotic biotransformation (2009), Expert. Opin. Drug Metab. Toxicol., 5, 1213-1221.
    View publication on PubMed
Search for more literature for 1.14.16.1

Protein Variants

Protein Variants Comment Organism
I65T the mutant shows increased specific activity using L-phenylalanine as substrate and decreased specific activity using S-carboxymethyl-L-cysteine compared to the wild type enzyme Homo sapiens
R261Q the mutant shows decreased specific activity using L-phenylalanine and S-carboxymethyl-L-cysteine as substrate compared to the wild type enzyme Homo sapiens
R68S the mutant shows decreased specific activity using L-phenylalanine and S-carboxymethyl-L-cysteine as substrate compared to the wild type enzyme Homo sapiens
V388M the mutant shows decreased specific activity using L-phenylalanine and S-carboxymethyl-L-cysteine as substrate compared to the wild type enzyme Homo sapiens
Y414C the mutant shows decreased specific activity using L-phenylalanine and S-carboxymethyl-L-cysteine as substrate compared to the wild type enzyme Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.022
-
 5,6,7,8-tetrahydrobiopterin mutant enzyme Y414C, using L-phenylalanine as cosubstrate Homo sapiens
0.024
-
 5,6,7,8-tetrahydrobiopterin mutant enzyme V388M, using L-phenylalanine as cosubstrate Homo sapiens
0.026
-
 5,6,7,8-tetrahydrobiopterin wild type enzyme, using L-phenylalanine as cosubstrate Homo sapiens
0.027
-
 5,6,7,8-tetrahydrobiopterin mutant enzyme R261Q, using L-phenylalanine as cosubstrate Homo sapiens
0.032
-
 5,6,7,8-tetrahydrobiopterin mutant enzyme R68S, using L-phenylalanine as cosubstrate Homo sapiens
0.04
-
 5,6,7,8-tetrahydrobiopterin mutant enzyme I65T, using L-phenylalanine as cosubstrate Homo sapiens
0.0728
-
 5,6,7,8-tetrahydrobiopterin wild type enzyme, using S-carboxymethyl-L-cysteine as cosubstrate Homo sapiens
0.14
-
 5,6,7,8-tetrahydrobiopterin mutant enzyme R68S, using S-carboxymethyl-L-cysteine as cosubstrate Homo sapiens
0.143
-
 5,6,7,8-tetrahydrobiopterin mutant enzyme Y414C, using S-carboxymethyl-L-cysteine as cosubstrate Homo sapiens
0.146
-
 5,6,7,8-tetrahydrobiopterin mutant enzyme V388M, using S-carboxymethyl-L-cysteine as cosubstrate Homo sapiens
0.15
-
 5,6,7,8-tetrahydrobiopterin mutant enzyme I65T, using S-carboxymethyl-L-cysteine as cosubstrate Homo sapiens
0.155
-
 5,6,7,8-tetrahydrobiopterin mutant enzyme R261Q, using S-carboxymethyl-L-cysteine as cosubstrate Homo sapiens
14.73
-
 S-carboxymethyl-L-cysteine wild type enzyme from hepatic cytosol Rattus norvegicus
16.53
-
 S-carboxymethyl-L-cysteine wild type enzyme from hepatic cytosol Homo sapiens
25.24
-
 S-carboxymethyl-L-cysteine wild type enzyme from Hep-G2 cell cytosol Homo sapiens
43.25
-
 S-methyl-L-cysteine wild type enzyme from hepatic cytosol Rattus norvegicus
44.63
-
 S-methyl-L-cysteine wild type enzyme from hepatic cytosol Homo sapiens
51.6
-
 S-methyl-L-cysteine wild type enzyme from Hep-G2 cell cytosol Homo sapiens
55.97
-
 N-acetyl-S-carboxymethyl-L-cysteine wild type enzyme from hepatic cytosol Rattus norvegicus
57.15
-
 N-acetyl-S-carboxymethyl-L-cysteine wild type enzyme from hepatic cytosol Homo sapiens
58.92
-
 N-acetyl-S-methyl-L-cysteine wild type enzyme from hepatic cytosol Rattus norvegicus
60.54
-
 N-acetyl-S-methyl-L-cysteine wild type enzyme from hepatic cytosol Homo sapiens
63.8
-
 N-acetyl-S-carboxymethyl-L-cysteine wild type enzyme from Hep-G2 cell cytosol Homo sapiens
68.25
-
 N-acetyl-S-methyl-L-cysteine wild type enzyme from Hep-G2 cell cytosol Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol
-
 Rattus norvegicus 5829
-
cytosol
-
 Homo sapiens 5829
-

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ contains one Fe2+ per monomer Rattus norvegicus
Fe2+ contains one Fe2+ per monomer Homo sapiens

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
52000
-
 calculated from sequence of cDNA Rattus norvegicus
52000
-
 calculated from sequence of cDNA Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens P00439
-
-
Rattus norvegicus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
Hep-G2 cell
-
 Homo sapiens
-
liver
-
 Rattus norvegicus
-
liver
-
 Homo sapiens
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.0009
-
 mutant enzyme V388M, using S-carboxymethyl-L-cysteine as substrate Homo sapiens
0.0014
-
 mutant enzyme I65T, using S-carboxymethyl-L-cysteine as substrate Homo sapiens
0.0014
-
 mutant enzyme R68S, using S-carboxymethyl-L-cysteine as substrate Homo sapiens
0.0015
-
 mutant enzyme Y414C, using S-carboxymethyl-L-cysteine as substrate Homo sapiens
0.0016
-
 mutant enzyme R261Q, using S-carboxymethyl-L-cysteine as substrate Homo sapiens
0.073
-
 wild type enzyme, using S-carboxymethyl-L-cysteine as substrate Homo sapiens
0.505
-
 mutant enzyme V388M, using L-phenylalanine as substrate Homo sapiens
1.2
-
 mutant enzyme Y414C, using L-phenylalanine as substrate Homo sapiens
1.49
-
 mutant enzyme R261Q, using L-phenylalanine as substrate Homo sapiens
1.725
-
 mutant enzyme R68S, using L-phenylalanine as substrate Homo sapiens
1.9
-
 wild type enzyme, using L-phenylalanine as substrate Homo sapiens
2.25
-
 mutant enzyme I65T, using L-phenylalanine as substrate Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-phenylalanine + 5,6,7,8-tetrahydrobiopterin + O2
-
 Rattus norvegicus L-tyrosine + 4a-hydroxytetrahydrobiopterin
-
 ?
L-phenylalanine + 5,6,7,8-tetrahydrobiopterin + O2
-
 Homo sapiens L-tyrosine + 4a-hydroxytetrahydrobiopterin
-
 ?
additional information thiodiglycolic acid is not a substrate for PAH Rattus norvegicus ?
-
 ?
additional information thiodiglycolic acid is not a substrate for PAH Homo sapiens ?
-
 ?
N-acetyl-S-carboxymethyl-L-cysteine + O2
-
 Rattus norvegicus ?
-
 ?
N-acetyl-S-carboxymethyl-L-cysteine + O2
-
 Homo sapiens ?
-
 ?
N-acetyl-S-methyl-L-cysteine + O2
-
 Rattus norvegicus ?
-
 ?
N-acetyl-S-methyl-L-cysteine + O2
-
 Homo sapiens ?
-
 ?
S-carboxymethyl-L-cysteine + tetrahydrobiopterin + O2
-
 Rattus norvegicus S-carboxymethyl-L-cysteine S-oxide + dihydrobiopterin + H2O
-
 ?
S-carboxymethyl-L-cysteine + tetrahydrobiopterin + O2
-
 Homo sapiens S-carboxymethyl-L-cysteine S-oxide + dihydrobiopterin + H2O
-
 ?
S-methyl-L-cysteine + O2
-
 Rattus norvegicus ?
-
 ?
S-methyl-L-cysteine + O2
-
 Homo sapiens ?
-
 ?

Subunits

Subunits Comment Organism
homotetramer
-
 Homo sapiens
homotetramer 4 * 52000, calculated from sequence of cDNA Rattus norvegicus

Synonyms

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

Cofactor

Cofactor Comment Organism Structure
5,6,7,8-tetrahydro-L-biopterin
-
 Rattus norvegicus
5,6,7,8-tetrahydro-L-biopterin
-
 Homo sapiens

General Information

General Information Comment Organism
physiological function key enzyme in the sulfoxidation of S-carboxymethyl-L-cysteine S-oxide and its thioester metabolites S-methyl-L-cysteine, N-acetyl-S-carboxymethyl-L-cysteine, and N-acetyl-S-methyl-L-cysteine Rattus norvegicus
physiological function key enzyme in the sulfoxidation of S-carboxymethyl-L-cysteine S-oxide and its thioester metabolites S-methyl-L-cysteine, N-acetyl-S-carboxymethyl-L-cysteine, and N-acetyl-S-methyl-L-cysteine Homo sapiens