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 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 | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
cytosol | - |
Rattus norvegicus | 5829 | - |
cytosol | - |
Homo sapiens | 5829 | - |
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 Maximum [Da] | Comment | Organism |
---|---|---|---|
52000 | - |
calculated from sequence of cDNA | Rattus norvegicus |
52000 | - |
calculated from sequence of cDNA | Homo sapiens |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | P00439 | - |
- |
Rattus norvegicus | - |
- |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
Hep-G2 cell | - |
Homo sapiens | - |
liver | - |
Rattus norvegicus | - |
liver | - |
Homo sapiens | - |
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 | 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 | Comment | Organism |
---|---|---|
homotetramer | - |
Homo sapiens |
homotetramer | 4 * 52000, calculated from sequence of cDNA | Rattus norvegicus |
Synonyms | Comment | Organism |
---|---|---|
PAH | - |
Rattus norvegicus |
PAH | - |
Homo sapiens |
phenylalanine hydroxylase | - |
Rattus norvegicus |
phenylalanine hydroxylase | - |
Homo sapiens |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
5,6,7,8-tetrahydro-L-biopterin | - |
Rattus norvegicus | |
5,6,7,8-tetrahydro-L-biopterin | - |
Homo sapiens |
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 |