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Synonyms
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2-hydroxyphenylpropionate hydroxylase
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2-hydroxyphenylpropionic hydroxylase
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melilotate hydroxylase
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melilotic hydroxylase
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oxygenase, melilotate 3-mono-
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3-(2-hydroxyphenyl)propanoate + NADH + H+ + O2 = 3-(2,3-dihydroxyphenyl)propanoate + NAD+ + H2O
3-(2-hydroxyphenyl)propanoate + NADH + H+ + O2 = 3-(2,3-dihydroxyphenyl)propanoate + NAD+ + H2O
mechanism
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3-(2-hydroxyphenyl)propanoate + NADH + H+ + O2 = 3-(2,3-dihydroxyphenyl)propanoate + NAD+ + H2O
mechanism
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3-(2-hydroxyphenyl)propanoate + NADH + H+ + O2 = 3-(2,3-dihydroxyphenyl)propanoate + NAD+ + H2O
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3-(2-hydroxyphenyl)propanoate,NADH:oxygen oxidoreductase (3-hydroxylating)
A flavoprotein (FAD).
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3-(2-hydroxyphenyl)propanoate + NADH + O2
3-(2,3-dihydroxyphenyl)propanoate + NAD+ + H2O
additional information
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Substrates: high specificity, low activity with 3-hydroxyphenylpropanoate with 20% of melilotate reduction, phenylpropanoate with 1-2% of meliotate reduction
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3-(2-hydroxyphenyl)propanoate + NADH + O2
3-(2,3-dihydroxyphenyl)propanoate + NAD+ + H2O
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Substrates: -
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3-(2-hydroxyphenyl)propanoate + NADH + O2
3-(2,3-dihydroxyphenyl)propanoate + NAD+ + H2O
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Substrates: i.e. melilotate, reversibility could not be demonstrated
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3-(2-hydroxyphenyl)propanoate + NADH + O2
3-(2,3-dihydroxyphenyl)propanoate + NAD+ + H2O
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Substrates: i.e. melilotate, role in metabolism of coumarin
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3-(2-hydroxyphenyl)propanoate + NADH + O2
3-(2,3-dihydroxyphenyl)propanoate + NAD+ + H2O
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Substrates: -
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3-(2-hydroxyphenyl)propanoate + NADH + O2
3-(2,3-dihydroxyphenyl)propanoate + NAD+ + H2O
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Substrates: i.e. melilotate, role in metabolism of coumarin
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FAD
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flavoprotein
FAD
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1 mol FAD per protein of MW 65000
FAD
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FAD: prosthetic group
FAD
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FAD: prosthetic group
NADH
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NADH
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uses the re-face of the flavin ring
NADH
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A-stereospecificity
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p-chloromercuribenzoate
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additional information
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not inhibitory: iodoacetic acid, iodoacetamide
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0.0027
3-(2-hydroxyphenyl)propanoate
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0.0013 - 0.086
melilotate
0.0013
melilotate
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0.0013
melilotate
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overview
0.0047
NADH
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0.02
O2
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stopped flow
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3.87 - 4.48
3-(2-hydroxyphenyl)propanoate
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5 - 9
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at pH 5.0 and 9.0: about 30% of maximum activity
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brenda
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brenda
Highest Expressing Human Cell Lines
Filter by:
Cell Line Links
Gene Links
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238000 - 250000
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238000 - 250000
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gel filtration, ultracentrifugation
65000
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65000
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sucrose density gradient centrifugation, gel filtration
65000
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4 * 65000, SDS-PAGE
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tetramer
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tetramer
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4 * 65000, SDS-PAGE
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enzyme is rapidly reduced by irradiation with visible light in presence of EDTA or by dithionite
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396421
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-20°C, stable for 1 week
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-20°C, stable for 3 weeks, highly purified enzyme, concentrated by dialysis
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-70°C, stable for 1 week
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activity can be restored with FAD
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Flashner, M.S.; Massey, V.
Flavoprotein oxygenases
Mol. Mech. Oxygen Activ. (Hayaishi, O., ed.) Academic Press, New York
245-283
1974
Arthrobacter sp., Pseudomonas sp.
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brenda
Levy, C.C.
Melilotate hydroxylase. Purification of the enzyme and the nature of the prosthetic group
J. Biol. Chem.
242
747-753
1967
Arthrobacter sp.
brenda
Strickland, S.; Massey, V.
The purification and properties of the flavoprotein melilotate hydroxylase
J. Biol. Chem.
248
2944-2952
1973
Pseudomonas sp.
brenda
Levy, C.C.; Frost, P.
The metabolism of coumarin by a microorganism. V. Melilotate hydroxylase
J. Biol. Chem.
241
997-1003
1966
Arthrobacter sp.
brenda
Strickland, S.; Massey, V.
The mechanism of action of the flavoprotein melilotate hydroxylase
J. Biol. Chem.
248
2953-2962
1973
Pseudomonas sp.
brenda
Strickland, S.; Schopfer, L.M.; Massey, V.
Kinetic and mechanistic studies on the reaction of melilotate hydroxylase with deuterated melilotate
Biochemistry
14
2230-2235
1975
Pseudomonas sp.
brenda
Schopfer, L.M.; Massey, V.
Kinetic and mechanistic studies on the reduction of melilotate hydroxylase by reduced pyridine nucleotides
J. Biol. Chem.
254
10634-10643
1979
Pseudomonas sp.
brenda
Manstein, D.J.; Pai, E.F.
Absolute stereochemistry of flavins in enzyme-catalyzed reactions
Biochemistry
25
6807-6816
1986
Pseudomonas sp.
brenda
You, K.S.; Arnold, L.J.; Kaplan, N.O.
The stereospecificity of bacterial external flavoprotein monooxygenases for nicotinamide adenine dinucleotide
Arch. Biochem. Biophys.
180
550-554
1977
Pseudomonas sp.
brenda
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