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Information on EC 1.13.11.27 - 4-hydroxyphenylpyruvate dioxygenase and Organism(s) Pseudomonas sp. and UniProt Accession P80064

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IUBMB Comments
The Pseudomonas enzyme contains one Fe3+ per mole of enzyme; the enzymes from other sources may contain essential iron or copper.
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This record set is specific for:
Pseudomonas sp.
UNIPROT: P80064
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The taxonomic range for the selected organisms is: Pseudomonas sp.
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
f protein, 4-hydroxyphenylpyruvate dioxygenase, tf-ag, p-hydroxyphenylpyruvate dioxygenase, 4-hppd, 4-hydroxyphenylpyruvic acid dioxygenase, 4hppd, athppd, p-hydroxyphenylpyruvate hydroxylase, legiolysin, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4-HPPD
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4-hydroxyphenylpyruvic acid dioxygenase
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4HPPD
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EC 1.14.2.2
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EC 1.99.1.14, formerly
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F Alloantigen
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F protein
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F-antigen homolog
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HPD
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HPPD
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HPPDase
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-
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Legiolysin
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oxygenase, 4-hydroxyphenylpyruvate di-
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p-hydroxyphenylpyruvate dioxygenase
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p-hydroxyphenylpyruvate hydroxylase
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p-hydroxyphenylpyruvate oxidase
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p-hydroxyphenylpyruvic acid hydroxylase
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p-hydroxyphenylpyruvic hydroxylase
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p-hydroxyphenylpyruvic oxidase
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T-cell reactive protein
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TF-AG
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-
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
4-hydroxyphenylpyruvate + O2 = homogentisate + CO2
show the reaction diagram
mono-iso-ordered bi-bi mechanism with binding of 4-hydroxyphenylpyruvate before O2 and release of CO2 before homogentisate. A Theorell-Chance mechanism can not be excluded
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decarboxylation
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redox reaction
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hydroxylation
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side-chain migration
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SYSTEMATIC NAME
IUBMB Comments
4-hydroxyphenylpyruvate:oxygen oxidoreductase (hydroxylating, decarboxylating)
The Pseudomonas enzyme contains one Fe3+ per mole of enzyme; the enzymes from other sources may contain essential iron or copper.
CAS REGISTRY NUMBER
COMMENTARY hide
9029-72-5
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(2-fluoro-4-hydroxyphenyl)pyruvate + O2
(3-fluoro-2,5-dihydroxyphenyl)pyruvate + CO2
show the reaction diagram
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-
-
?
4-hydroxyphenylpyruvate + O2
homogentisate + CO2
show the reaction diagram
phenylpyruvate + O2
2-hydroxyphenylacetate + CO2
show the reaction diagram
[(4-hydroxyphenyl)thio]pyruvate + O2
[(4-hydroxyphenyl)sulfinyl]acetate + CO2
show the reaction diagram
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substrate undergoes oxidative decarboxylation and sulfoxidation to give [(4-hydroxyphenyl)sulfinyl]acetate, ring oxidation is not observed
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-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
copper
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variable amounts of copper: 0.2-0.5 mol per mol of enzyme
Fe3+
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iron in the Fe3+ form must be reduced for enzyme activity
Zinc
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0.68 mol of zinc per mol of enzyme
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(2,6-difluoro-4-hydroxyphenyl)pyruvate
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competitive, most potent
1,2-dihydroxybenzene
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0.019 mM, 50% inhibition, uncompetitive
1,2-dihydroxybenzene-3,5-disulfonic acid
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inhibition is prevented by ascorbate but not reversed by enol-4-hydroxyphenylpyruvate
1,4-benzoquinone
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0.25 mM, 50% inhibition, competitive
1,4-dihydroxybenzene
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4.7 mM, 50% inhibition
2,2'-bipyridyl
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0.32 mM, 50% inhibition
2,4-Dihydroxybenzoate
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4.2 mM, 50% inhibition, noncompetitive
2,5-Dihydroxybenzoate
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2.6 mM, 50% inhibition, noncompetitive
2,5-dihydroxyphenylacetate
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50% inhibition above 10 mM, noncompetitive
2,5-dihydroxyphenylacetic acid lactone
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50% inhibition above 10 mM, competitive
2-hydroxyphenylacetate
3,4-dihydroxybenzoate
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0.24 mM, 50% inhibition, noncompetitive
3,4-Dihydroxyphenylacetate
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0.75 mM, 50% inhibition, noncompetitive
3,5-diiodo-4-hydroxyphenylpyruvate
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0.25 mM, 50% inhibition, competitive
3-(2-hydroxyphenyl)propionate
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50% inhibition above 10 mM, competitive
3-methoxy-4-hydroxyphenylacetate
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0.25 mM, 50% inhibition, competitive
4-hydroxybenzaldehyde
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50% inhibition above 10 mM, noncompetitive
4-hydroxyphenylpyruvate
8-Hydroxyquinoline-5-sulfonic acid
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560 nM, 50% inhibition
Acetopyruvate
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0.33 mM, 50% inhibition, competitive
Bathocuproine
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3 mM, 50% inhibition
bathophenanthroline
citrate
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Cupferron
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0.0071 mM, 50% inhibition
diethyl dicarbonate
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5 mM, 50% inhibition
diethyldithiocarbamate
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0.0021 mM, 50% inhibition
DL-3,4-dihydroxyphenylalanine
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0.32 mM, 50% inhibition, noncompetitive
DL-4-hydroxyphenyllactate
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50% inhibition above 10 mM, competitive
DL-Epinephrine
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0.17 mM, 50% inhibition, noncompetitive
ethanol
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5% v/v, 50% inhibition, complete loss of activity at 20% v/v
homogentisate
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product inhibition
L-Phe
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10 mM, 50% inhibition, competitive
oxaloacetate
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10 mM, 50% inhibition, noncompetitive
phenylglyoxalate
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50% inhibition above 10 mM, competitive
phenylpyruvate
pyridoxal 5'-phosphate
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2 mM, 50% inhibition
pyruvate
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50% inhibition above 10 mM, competitive
Tiron
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0.4 mM, 50% inhibition
trans-4-hydroxycinnamate
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50% inhibition above 10 mM, competitive
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,6-dichlorophenol indophenol
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competitive activator
ascorbate
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an optimized combination of ascorbate, 50 mM, catalase, 2.4 g/l, and iron, 0.05 mM, activates more than a combination of 2,6-dichlorophenolindophenol, glutathione and catalase
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.03
4-hydroxyphenylpyruvate
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0.5 - 0.52
phenylpyruvate
additional information
additional information
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0013
(2,6-difluoro-4-hydroxyphenyl)pyruvate
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-
additional information
additional information
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 9.5
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pH 6.0: about 55% of maximal activity, pH 9.5: about 50% of maximal activity
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
150000
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high-speed equilibrium sedimentation
36000
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4 * 36000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
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4 * 36000, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging-drop method in 18-25% PEG 4000, 0.2 M ammonium acetate, 0.1 M trisodium citrate, pH 5.6, at room temperature
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 8
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37°C, 15 min, stable
395375
7.5
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37°C, 7.5 min, stable
395376
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-60°C, 0.2 M NaCl solution buffered with 10 mM potassium phosphate, pH 6.7, stable for several months
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-60°C, stable for several months
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme expressed in Escherichia coli
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lindstedt, S.; Odelhoeg, B.
4-Hydroxyphenylpyruvate dioxygenase from Pseudomonas
Methods Enzymol.
142
143-148
1987
Pseudomonas sp., Pseudomonas sp. P.J. 874
Manually annotated by BRENDA team
Bradley, F.C.; Lindstedt, S.; Lipscomb, J.D.; Que, L.; Lawrence, A.; Rundgren, M.
4-Hydroxyphenylpyruvate dioxygenase is an iron-tyrosinate protein
J. Biol. Chem.
261
11693-11698
1986
Pseudomonas sp., Pseudomonas sp. P.J. 874
Manually annotated by BRENDA team
Pascal, R.A.; Oliver, M.A.; Chen, Y.C.J.
Alternate substrates and inhibitors of bacterial 4-hydroxyphenylpyruvate dioxygenase
Biochemistry
24
3158-3165
1985
Pseudomonas sp., Pseudomonas sp. P.J. 874
Manually annotated by BRENDA team
Rundgren, M.
Some kinetic properties of 4-hydroxyphenylpyruvate dioxygenase from Pseudomonas sp. strain P.J. 874
Eur. J. Biochem.
133
657-663
1983
Pseudomonas sp., Pseudomonas sp. P.J. 874
Manually annotated by BRENDA team
Lindstedt, S.; Rundgren, M.
Blue color, metal content, and substrate binding in 4-hydroxyphenylpyruvate dioxygenase from Pseudomonas sp. strain P. J. 874
J. Biol. Chem.
257
11922-11931
1982
Pseudomonas sp.
Manually annotated by BRENDA team
Lindstedt, S.; Rundgren, M.
Inhibition of 4-hydroxyphenylpyruvate dioxygenase from Pseudomonas sp. strain P.J. 874 the enol tautomer of the substrate
Biochim. Biophys. Acta
704
66-74
1982
Pseudomonas sp., Pseudomonas sp. P.J. 874
Manually annotated by BRENDA team
Lindstedt, S.; Odelhoeg, B.; Rundgren, M.
Purification and some properties of 4-hydroxyphenylpyruvate dioxygenase from Pseudomonas sp. P. J. 874
Biochemistry
16
3369-3377
1977
Pseudomonas sp., Pseudomonas sp. P.J. 874
Manually annotated by BRENDA team
Serre, L.; Sailland, A.; Sy, D.; Boudec, P.; Rolland, A.; Pebay-Peyroula, E.; Cohen-Addad, C.
Crystal structure of Pseudomonas fluorescens 4-hydroxyphenylpyruvate dioxygenase: an enzyme involved in the tyrosine degradation pathway
Structure Fold. Des.
7
977-988
1999
Pseudomonas sp.
Manually annotated by BRENDA team