Literature summary 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.

KM Value [mM]

EC Number	KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
1.14.16.1	0.0024	-	L-cyclohexylalanine	-	Chromobacterium violaceum

Organism

EC Number	Organism	UniProt	Comment	Textmining
1.14.16.1	Chromobacterium violaceum	-	-	-
1.14.16.1	Rattus norvegicus	-	-	-

Purification (Commentary)

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

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
1.14.16.1	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	?
1.14.16.1	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	?
1.14.16.1	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	-	?
1.14.16.1	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	-	?

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Release 2023.1 (January 2023)