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Literature summary for 1.14.16.1 extracted from

  • Volner, A.; Zoidakis, J.; Abu-Omar, M.M.
    Order of substrate binding in bacterial phenylalanine hydroxylase and its mechanistic implication for pterin-dependent oxygenases (2003), J. Biol. Inorg. Chem., 8, 121-128.
    View publication on PubMed

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.044
-
6,7-dimethyl-5,6,7,8-tetrahydrobiopterin
-
Chromobacterium violaceum
0.059
-
L-phenylalanine
-
Chromobacterium violaceum
0.076
-
O2
-
Chromobacterium violaceum

Metals/Ions

Metals/Ions Comment Organism Structure
Iron
-
Chromobacterium violaceum

Organism

Organism UniProt Comment Textmining
Chromobacterium violaceum P30967
-
-

Reaction

Reaction Comment Organism Reaction ID
L-phenylalanine + a 5,6,7,8-tetrahydropteridine + O2 = L-tyrosine + a 4a-hydroxy-5,6,7,8-tetrahydropteridine sequential ter-bi mechansim, L-phenylalanine is the middle substrate in order of binding Chromobacterium violaceum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-phenylalanine + 6,7-dimethyl-5,6,7,8-tetrahydrobiopterin + O2
-
Chromobacterium violaceum L-tyrosine + 7,8-dimethyl-6,7-dihydrobiopterin + H2O
-
?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3 6 6,7-dimethyl-5,6,7,8-tetrahydrobiopterin
-
Chromobacterium violaceum

Cofactor

Cofactor Comment Organism Structure
6,7-dimethyl-5,6,7,8-tetrahydrobiopterin
-
Chromobacterium violaceum