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Literature summary for 1.14.16.1 extracted from

  • Carr, R.T.; Balasubramanian, S.; Hawkins, P.C.D.; Benkovic, S.J.
    Mechanism of metal-independent hydroxylation by Chromobacterium violaceum phenylalanine hydroxylase (1995), Biochemistry, 34, 7525-7532.
    View publication on PubMed

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0024
-
L-cyclohexylalanine
-
Chromobacterium violaceum

Organism

Organism UniProt Comment Textmining
Chromobacterium violaceum
-
-
-
Rattus norvegicus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
metal-free enzyme by extraction of copper with dithiothreitol Chromobacterium violaceum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-methylphenylalanine + 6,7-dimethyl-tetrahydropterin + O2
-
Chromobacterium violaceum 4-(hydroxymethyl)phenylalanine + 3-methyltyrosine + H2O + 6,7-dimethyl-dihydropterin 74% methyl-hydroxylation, 26% para-hydroxylation, shift of para-substituent by NIH shift mechanism ?
4-methylphenylalanine + 6,7-dimethyl-tetrahydropterin + O2
-
Rattus norvegicus 4-(hydroxymethyl)phenylalanine + 3-methyltyrosine + H2O + 6,7-dimethyl-dihydropterin 79% methyl-hydroxylation, 21% para-hydroxylation, shift of para-substituent by NIH shift mechanism ?
L-cyclohexylalanine + 6,7-dimethyl-tetrahydropterin + O2 4times slower reaction than with L-phenylalanine Chromobacterium violaceum 4-hydroxy-L-cyclohexylalanine + H2O + 6,7-dimethyl-dihydropterin
-
?
L-cyclohexylalanine + 6,7-dimethyl-tetrahydropterin + O2 50% less active than the enzyme from Chromobacterium violaceum Rattus norvegicus 4-hydroxy-L-cyclohexylalanine + H2O + 6,7-dimethyl-dihydropterin
-
?