Literature summary for 1.14.16.1 extracted from

Pember, S.O.; Villafranca, J.J.; Benkovic, S.J.
Phenylalanine hydroxylase from Chromobacterium violaceum is a copper-containing monooxygenase. Kinetics of the reductive activation of the enzyme (1986), Biochemistry, 25, 6611-6619.

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Metals/Ions

Metals/Ions	Comment	Organism	Structure
copper	electron paramagnetic resonance spectroscopy indicates a type II copper-containing enzyme	Chromobacterium violaceum
copper	1 mol of Cu2+ per mol of enzyme	Chromobacterium violaceum

Organism

Organism	UniProt	Comment	Textmining
Chromobacterium violaceum	-	-	-

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	enzyme requires an initial reduction of Cu2+ to Cu+ for activation	Chromobacterium violaceum	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
L-phenylalanine + tetrahydrobiopterin + O2	-	Chromobacterium violaceum	L-tyrosine + dihydrobiopterin + H2O	-	?

Cofactor

Cofactor	Comment	Organism	Structure
tetrahydrobiopterin	-	Chromobacterium violaceum

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Release 2023.1 (January 2023)