Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Steventon, G.B.; Mitchell, S.C.; Perez, B.; Desviat, L.R.; Ugarte, M.
    The activity of wild type and mutant phenylalanine hydroxylase with respect to the C-oxidation of phenylalanine and the S-oxidation of S-carboxymethyl-L-cysteine (2009), Mol. Genet. Metab., 96, 27-31.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.14.16.1 mutant enzymes are expressed in Escherichia coli Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
1.14.16.1 I174T the mutation results in the classical phenylketonuria phenotype expressing 0.2-1.8% of the wild type PAH activity when using L-phenylalanine as substrate, and has less 0.1% of the wild type PAH activity when S-carboxymethyl-L-cysteine is used as the substrate Homo sapiens
1.14.16.1 I65T the S-oxidation of S-carboxymethyl-L-cysteine is dramatically reduced in the 5,6,7,8-tetrahydro-L-biopterin responsive mutant I65T possessing 1.2-2.0% of the wild type PAH activity when S-carboxymethyl-L-cysteine is used as substrate and expressing 23-76% of the wild type PAH activity when L-phenylalanine is used as the substrate Homo sapiens
1.14.16.1 R158Q the mutation results in the classical phenylketonuria phenotype expressing 0.2-1.8% of the wild type PAH activity when using L-phenylalanine as substrate, and has less 0.1% of the wild type PAH activity when S-carboxymethyl-L-cysteine is used as the substrate Homo sapiens
1.14.16.1 R261Q the S-oxidation of S-carboxymethyl-L-cysteine is dramatically reduced in the 5,6,7,8-tetrahydro-L-biopterin responsive mutant I65T possessing 1.2-2.0% of the wild type PAH activity when S-carboxymethyl-L-cysteine is used as substrate and expressing 23-76% of the wild type PAH activity when L-phenylalanine is used as the substrate Homo sapiens
1.14.16.1 R408W the mutation results in the classical phenylketonuria phenotype expressing 0.2-1.8% of the wild type PAH activity when using L-phenylalanine as substrate, and has less 0.1% of the wild type PAH activity when S-carboxymethyl-L-cysteine is used as the substrate Homo sapiens
1.14.16.1 R68S the S-oxidation of S-carboxymethyl-L-cysteine is dramatically reduced in the 5,6,7,8-tetrahydro-L-biopterin responsive mutant I65T possessing 1.2-2.0% of the wild type PAH activity when S-carboxymethyl-L-cysteine is used as substrate and expressing 23-76% of the wild type PAH activity when L-phenylalanine is used as the substrate Homo sapiens
1.14.16.1 V388M the S-oxidation of S-carboxymethyl-L-cysteine is dramatically reduced in the 5,6,7,8-tetrahydro-L-biopterin responsive mutant I65T possessing 1.2-2.0% of the wild type PAH activity when S-carboxymethyl-L-cysteine is used as substrate and expressing 23-76% of the wild type PAH activity when L-phenylalanine is used as the substrate Homo sapiens
1.14.16.1 Y414C the S-oxidation of S-carboxymethyl-L-cysteine is dramatically reduced in the 5,6,7,8-tetrahydro-L-biopterin responsive mutant I65T possessing 1.2-2.0% of the wild type PAH activity when S-carboxymethyl-L-cysteine is used as substrate and expressing 23-76% of the wild type PAH activity when L-phenylalanine is used as the substrate Homo sapiens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.14.16.1 0.022
-
 L-phenylalanine mutant enzyme Y414C, in 50 mM potassium phosphate buffer (pH 6.8), at 37°C Homo sapiens
1.14.16.1 0.024
-
 L-phenylalanine mutant enzyme V388M, in 50 mM potassium phosphate buffer (pH 6.8), at 37°C Homo sapiens
1.14.16.1 0.026
-
 L-phenylalanine wild type enzyme, in 50 mM potassium phosphate buffer (pH 6.8), at 37°C Homo sapiens
1.14.16.1 0.027
-
 L-phenylalanine mutant enzyme R261Q, in 50 mM potassium phosphate buffer (pH 6.8), at 37°C Homo sapiens
1.14.16.1 0.032
-
 L-phenylalanine mutant enzyme R68S, in 50 mM potassium phosphate buffer (pH 6.8), at 37°C Homo sapiens
1.14.16.1 0.04
-
 L-phenylalanine mutant enzyme I65T, in 50 mM potassium phosphate buffer (pH 6.8), at 37°C Homo sapiens
1.14.16.1 0.0728
-
 S-carboxymethyl-L-cysteine wild type enzyme, in 50 mM potassium phosphate buffer (pH 6.8), at 37°C Homo sapiens
1.14.16.1 0.14
-
 S-carboxymethyl-L-cysteine mutant enzyme R68S, in 50 mM potassium phosphate buffer (pH 6.8), at 37°C Homo sapiens
1.14.16.1 0.143
-
 S-carboxymethyl-L-cysteine mutant enzyme Y414C, in 50 mM potassium phosphate buffer (pH 6.8), at 37°C Homo sapiens
1.14.16.1 0.146
-
 S-carboxymethyl-L-cysteine mutant enzyme V388M, in 50 mM potassium phosphate buffer (pH 6.8), at 37°C Homo sapiens
1.14.16.1 0.15
-
 S-carboxymethyl-L-cysteine mutant enzyme I65T, in 50 mM potassium phosphate buffer (pH 6.8), at 37°C Homo sapiens
1.14.16.1 0.155
-
 S-carboxymethyl-L-cysteine mutant enzyme R261Q, in 50 mM potassium phosphate buffer (pH 6.8), at 37°C Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
1.14.16.1 Homo sapiens P00439
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.16.1 L-phenylalanine + 5,6,7,8-tetrahydro-L-biopterin + O2
-
 Homo sapiens L-tyrosine + 4a-hydroxytetrahydrobiopterin
-
 ?
1.14.16.1 additional information does not use thiodiglycolic acid as substrate Homo sapiens ?
-
 ?
1.14.16.1 N-acetyl-(S)-carboxymethyl-L-cysteine + 5,6,7,8-tetrahydro-L-biopterin + O2
-
 Homo sapiens N-acetyl-(S)-carboxymethyl-L-cysteine S-oxide + ?
-
 ?
1.14.16.1 N-acetyl-(S)-methyl-L-cysteine + 5,6,7,8-tetrahydro-L-biopterin + O2
-
 Homo sapiens N-acetyl-(S)-methyl-L-cysteine S-oxide + ?
-
 ?
1.14.16.1 S-carboxymethyl-L-cysteine + 5,6,7,8-tetrahydro-L-biopterin + O2
-
 Homo sapiens S-carboxymethyl-L-cysteine S-oxide + dihydrobiopterin + H2O
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.14.16.1 PAH
-
 Homo sapiens
1.14.16.1 phenylalanine hydroxylase
-
 Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.16.1 5,6,7,8-tetrahydro-L-biopterin
-
 Homo sapiens