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Literature summary for 1.14.16.7 extracted from

  • Zhang, W.; Ames, B.D.; Walsh, C.T.
    Identification of phenylalanine 3-hydroxylase for meta-tyrosine biosynthesis (2011), Biochemistry, 50, 5401-5403.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.14.16.7

Activating Compound

Activating Compound Comment Organism Structure
dithiothreitol increases the product yield more than 72% Streptomyces coeruleorubidus

Cloned(Commentary)

Cloned (Comment) Organism
cloned as an N-terminal six-His-tagged protein, expressed in Escherichia coli, wild-type and mutant enzymes C187F, T202G and C187F/T202G Streptomyces coeruleorubidus

Protein Variants

Protein Variants Comment Organism
C187F hydroxylation rate is reduced to less than 4% compared to the rate of wild-type enzyme Streptomyces coeruleorubidus
C187F/T202G hydroxylation rate is comparable to that of wild-type enzyme. Less than 8% of m-Tyr compared to p-Tyr is formed Streptomyces coeruleorubidus
T202G hydroxylation rate is comparable to that of wild-type enzyme. The ratio of product p-Tyr to m-Tyr is changed to 2:1 for the T202G mutant, which represents a 60-fold increase in the preference for p-Tyr over m-Tyr formation Streptomyces coeruleorubidus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.026
-
 6-methyltetrahydropterin pH 6.2, 22°C Streptomyces coeruleorubidus
1.1
-
 L-phenylalanine pH 6.2, 22°C Streptomyces coeruleorubidus

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ addition of ferrous ammonium sulfate increases the product yield more than 3-fold Streptomyces coeruleorubidus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-phenylalanine + tetrahydrobiopterin + O2 Streptomyces coeruleorubidus the enzyme forms 3-hydroxy-L-phenylalanine (i.e. m-L-tyrosine) which is one of the building blocks in the biosynthesis of pacidamycins 3-hydroxy-L-phenylalanine + 4a-hydroxytetrahydrobiopterin 3-hydroxy-L-phenylalanine i.e. m-L-Tyr ?

Organism

Organism UniProt Comment Textmining
Streptomyces coeruleorubidus F5BFC8
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Streptomyces coeruleorubidus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-phenylalanine + 6-methyltetrahydropterin + O2
-
 Streptomyces coeruleorubidus 3-hydroxy-L-phenylalanine + 4a-hydroxy-6-methyltetrahydropterin
-
 ?
L-phenylalanine + tetrahydrobiopterin + O2 the enzyme forms 3-hydroxy-L-phenylalanine (i.e. m-L-tyrosine) which is one of the building blocks in the biosynthesis of pacidamycins Streptomyces coeruleorubidus 3-hydroxy-L-phenylalanine + 4a-hydroxytetrahydrobiopterin 3-hydroxy-L-phenylalanine i.e. m-L-Tyr ?
additional information no activity with D-Phe, L-Tyr, and L-Trp Streptomyces coeruleorubidus ?
-
 ?

Synonyms

Synonyms Comment Organism
PacX
-
 Streptomyces coeruleorubidus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
22
-
 assay at Streptomyces coeruleorubidus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.021
-
 6-methyltetrahydropterin pH 6.2, 22°C Streptomyces coeruleorubidus
0.022
-
 L-phenylalanine pH 6.2, 22°C Streptomyces coeruleorubidus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6
-
-
 Streptomyces coeruleorubidus

General Information

General Information Comment Organism
physiological function the enzyme forms 3-hydroxy-L-phenylalanine (i.e. m-L-tyrosine) which is one of the building blocks in the biosynthesis of pacidamycins Streptomyces coeruleorubidus