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Literature summary for 1.14.16.1 extracted from

  • Ronau, J.A.; Paul, L.N.; Fuchs, J.E.; Liedl, K.R.; Abu-Omar, M.M.; Das, C.
    A conserved acidic residue in phenylalanine hydroxylase contributes to cofactor affinity and catalysis (2014), Biochemistry, 53, 6834-6848 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.14.16.1

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli Chromobacterium violaceum

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging drop vapor diffusion method Chromobacterium violaceum

Protein Variants

Protein Variants Comment Organism
D139A the catalytic efficiency for L-phenylalanine is 81fold lower than that of the wild type enzyme Chromobacterium violaceum
D139E the catalytic efficiency for L-phenylalanine is 7fold lower than that of the wild type enzyme Chromobacterium violaceum
D139K inactive Chromobacterium violaceum
D139N the catalytic efficiency for L-phenylalanine is 17fold lower than that of the wild type enzyme Chromobacterium violaceum

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.137
-
 L-phenylalanine mutant enzyme D139N, at pH 7.4 and 20°C Chromobacterium violaceum
0.152
-
 6,7-dimethyl-5,6,7,8-tetrahydropterin wild type enzyme, at pH 7.4 and 20°C Chromobacterium violaceum
0.225
-
 L-phenylalanine mutant enzyme D139N, at pH 7.4 and 20°C Chromobacterium violaceum
0.236
-
 6,7-dimethyl-5,6,7,8-tetrahydropterin mutant enzyme D139N, at pH 7.4 and 20°C Chromobacterium violaceum
0.244
-
 L-phenylalanine wild type enzyme, at pH 7.4 and 20°C Chromobacterium violaceum
0.254
-
 6,7-dimethyl-5,6,7,8-tetrahydropterin mutant enzyme D139N, at pH 7.4 and 20°C Chromobacterium violaceum
0.262
-
 6,7-dimethyl-5,6,7,8-tetrahydropterin mutant enzyme D139N, at pH 7.4 and 20°C Chromobacterium violaceum
0.316
-
 L-phenylalanine mutant enzyme D139N, at pH 7.4 and 20°C Chromobacterium violaceum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-phenylalanine + tetrahydrobiopterin + O2 Chromobacterium violaceum
-
 L-tyrosine + 4a-hydroxytetrahydrobiopterin
-
 ?

Organism

Organism UniProt Comment Textmining
Chromobacterium violaceum P30967
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-phenylalanine + 6,7-dimethyl-5,6,7,8-tetrahydropterin + O2
-
 Chromobacterium violaceum L-tyrosine + 4a-hydroxytetrahydrobiopterin
-
 ?
L-phenylalanine + tetrahydrobiopterin + O2
-
 Chromobacterium violaceum L-tyrosine + 4a-hydroxytetrahydrobiopterin
-
 ?

Synonyms

Synonyms Comment Organism
PAH
-
 Chromobacterium violaceum
phenylalanine hydroxylase
-
 Chromobacterium violaceum

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.59
-
 L-phenylalanine mutant enzyme D139N, at pH 7.4 and 20°C Chromobacterium violaceum
0.8
-
 6,7-dimethyl-5,6,7,8-tetrahydropterin mutant enzyme D139N, at pH 7.4 and 20°C Chromobacterium violaceum
2.8
-
 L-phenylalanine mutant enzyme D139N, at pH 7.4 and 20°C Chromobacterium violaceum
5.1
-
 6,7-dimethyl-5,6,7,8-tetrahydropterin mutant enzyme D139N, at pH 7.4 and 20°C Chromobacterium violaceum
7.1
-
 L-phenylalanine mutant enzyme D139N, at pH 7.4 and 20°C Chromobacterium violaceum
9.4
-
 6,7-dimethyl-5,6,7,8-tetrahydropterin mutant enzyme D139N, at pH 7.4 and 20°C Chromobacterium violaceum
48
-
 L-phenylalanine wild type enzyme, at pH 7.4 and 20°C Chromobacterium violaceum
130
-
 6,7-dimethyl-5,6,7,8-tetrahydropterin wild type enzyme, at pH 7.4 and 20°C Chromobacterium violaceum