Information on EC 1.13.11.27 - 4-hydroxyphenylpyruvate dioxygenase

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The expected taxonomic range for this enzyme is: Eukaryota, Archaea, Bacteria

EC NUMBER
COMMENTARY hide
1.13.11.27
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RECOMMENDED NAME
GeneOntology No.
4-hydroxyphenylpyruvate dioxygenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
4-hydroxyphenylpyruvate + O2 = homogentisate + CO2
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decarboxylation
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hydroxylation
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redox reaction
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side-chain migration
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
L-phenylalanine biosynthesis III (cytosolic, plants)
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L-phenylalanine degradation IV (mammalian, via side chain)
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L-tyrosine degradation I
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plastoquinol-9 biosynthesis I
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vitamin E biosynthesis (tocopherols)
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tyrosine metabolism
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Ubiquinone and other terpenoid-quinone biosynthesis
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Tyrosine metabolism
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Phenylalanine metabolism
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Metabolic pathways
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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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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Automatic Mining of ENzyme DAta
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Manually annotated by BRENDA team
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
bat
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
Frog
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Manually annotated by BRENDA team
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
Pseudomonas sp. P.J. 874
strain P.J. 874
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Manually annotated by BRENDA team
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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1047183 A+, 1047185 A+, 1047229 A+, 1047235 A+, 1047239 A+, 1047244 A+, 1047254 A+, 1047270 A+, 1047288 A+, 1047290 A+, 1047306 A+, 1047322 A+, 1047328 A+, 1047329 A+, 1047332 A+, 1047341 A+, 1047343 A+, 1047344 A+, 1047354 A+, 1249961 A+, 1297694 A+, 1297810 A+, 1297870 A+, 1324863 A+, 1456844 A+, 1520979 A+, 1596331 A+, 1607473 A+, 1607873 A+, 1607965 A+, 1615910 A+, 1767335 A+, 1767342 A+, 1767372 A+, 1767378 A+, 1767448 A+, 1767456 A+, 1767462 A+, 1767470 A+, 1767480 A+, 1767482 A+, 1767489 A+, 1767497 A+, 1767500 A+, 1767515 A+, 1767522 A+, 1767523 A+, 1767524 A+, 1767529 A+, 1767546 A+, 1767563 A+, 1767568 A+, 1767591 A+, 1767595 A+, 1767603 A+, 1767606 A+, 1767614 A+, 1767615 A+, 1767622 A+, 1767624 A+, 1767627 A+, 1767648 A+, 1767649 A+, 1767657 A+, 1767672 A+, 1767674 A+, 1767675 A+, 1767676 A+, 1767678 A+, 1767679 A+, 1767688 A+, 1767697 A+, 1767705 A+, 1767707 A+, 1767708 A+, 1767711 A+, 1767712 A+, 1767713 A+, 1767722 A+, 1767743 A+, 1767748 A+, 1767757 A+, 1767760 A+, 1767764 A+, 1767769 A+, 1767770 A+, 1767773 A+, 1767788 A+, 1767791 A+, 1767792 A+, 1767793 A+, 1767795 A+, 1767800 A+, 1767804 A+, 1767808 A+, 1767809 A+, 1767812 A+, 1767813 A+, 1767831 A+, 1767843 A+, 1767849 A+, 1767867 A+, 1767868 A+, 1767875 A+, 1767876 A+, 1767878 A+, 1767883 A+, 1767886 A+, 1767887 A+, 1767896 A+, 1767899 A+, 1767908 A+, 2770596 A+, 2814027 A+, 2814060 A+, 2814066 A+, 2814070 A+, 2814076 A+, 2814093 A+, 2814099 A+, 760223 A+, 760231 A+, 760255 A+, 897158 A+, 919192 A+, 1047327 A+++
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
salmon
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
Vitis vinifera x Vitis vinifera
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
deficiency in active 4-HPPD in humans results in type III tyrosinemia, a rare autosomal recessive disorder
metabolism
physiological function
additional information
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
(4-hydroxyphenyl)-pyruvate + O2
homogentisate + CO2
show the reaction diagram
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?
2-thienylpyruvate + O2
? + CO2
show the reaction diagram
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?
3,4-dihydroxyphenylpyruvate + O2
? + CO2
show the reaction diagram
3-thienylpyruvate + O2
3-carboxymethyl-3-thiolene-2-one + CO2
show the reaction diagram
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?
4-fluorophenylpyruvate + O2
4-fluoro-2-hydroxyphenylacetate + CO2
show the reaction diagram
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?
4-hydroxyphenylpyruvate + O2
2,5-dihydroxyphenylacetate + CO2
show the reaction diagram
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?
4-hydroxyphenylpyruvate + O2
homogentisate + CO2
show the reaction diagram
4-hydroxyphenylpyruvate + O2
homogentisate + CO2 + 4-hydroxyphenylacetate
show the reaction diagram
4-hydroxytetrafluorophenylpyruvate + O2
? + CO2
show the reaction diagram
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?
4-methylphenylpyruvate + O2
? + CO2
show the reaction diagram
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poor substrate
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?
phenylpyruvate + O2
2-hydroxyphenylacetate + CO2
show the reaction diagram
[(4-hydroxyphenyl)thio]pyruvate + O2
[(4-hydroxyphenyl)sulfinyl]acetate + CO2
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
4-hydroxyphenylpyruvate + O2
2,5-dihydroxyphenylacetate + CO2
show the reaction diagram
P80064
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?
4-hydroxyphenylpyruvate + O2
homogentisate + CO2
show the reaction diagram
4-hydroxyphenylpyruvate + O2
homogentisate + CO2 + 4-hydroxyphenylacetate
show the reaction diagram
additional information
?
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HpdR positively regulates hpdA expression through direct binding to the HpdA promoter within a region containing two conserved direct repeat sequences. HpdR-dependent hpdA transcription occurs in the presence of 4-hydroxyphenylpyruvate, tyrosine, and phenylalanine, as well as during starvation
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
copper
Zinc
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0.68 mol of zinc per mol of enzyme
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(2,6-difluoro-4-hydroxyphenyl)pyruvate
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competitive, most potent
1,10-phenanthroline
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
1-(1,1-dimethylethyl)-5-hydroxy-4-(3-(4-(methoxy)phenyl)-2-methyl-4-(methylsulfonyl)benzoyl)pyrazole
1-(2'-theonyl)-2,3-trifluoroacetone
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0.0049 mM, 50% inhibition
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1-(2'-thionyl)-3,3,3-trifluoroacetone
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2,2'-bipyridyl
2,4-Dihydroxybenzoate
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4.2 mM, 50% inhibition, noncompetitive
2,4-Dihydroxyphenylpyruvate
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competitive
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-(2-chloro-4-methane sulfonylbenzoyl)-1,3-cyclohexanedione
competitive inhibitor
2-(2-chloro-4-methanesulfonylbenzoyl)-1,3-cyclohexanedione
2-(2-nitro-4-(trifluoromethyl)benzoyl)-1,3-cyclohexanedione
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(NTBC), binding constant of 937 microM
2-(2-nitro-4-chlorobenzoyl)-5-(2-methoxyethyl)cyclohexane-1,3-dione
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2-Hydroxybenzaldehyde
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competitive
2-hydroxyphenylacetate
2-Hydroxyphenylpyruvate
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competitive
2-mercaptoethanol
10 mM, 65% inhibition
2-thienylpyruvate
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mechanism-based inhibitor
2-[2-nitro-4-(trifluoromethyl)benzoyl]-1,3-cyclohexanedione
2-[2-nitro-4-(trifluoromethyl)benzoyl]-4,4,6,6-tetramethylcyclohexane-1,3,5-trione
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50 nM, 50% inhibition, tight-binding reversible inhibitor, rapid inactivation by the formation of an enzyme-inhibitor complex that dissociates extremely slowly with recovery of enzyme activity
3,3,5,5-tetramethyl-2,4,6-trioxocyclohexyl 3-methylbutanoate
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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-cyclohexylethyl)-5,5,7,7-tetramethylbenzo[d]isoxazole-4,6(5H,7H)-dione
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3-(2-hydroxyphenyl)propionate
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50% inhibition above 10 mM, competitive
3-cyclohexyl-1-(2,4,6-trihydroxy-3-(3-methylbut-2-enyl)phenyl)propan-1-one
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3-hydroxy-4-phenyl-2-furanone
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0.0005 mM, 50% inhibition, may serve as a lead compound for further design of more potent inhibitors
3-hydroxyphenylpyruvate
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competitive
3-methoxy-4-hydroxyphenylacetate
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0.25 mM, 50% inhibition, competitive
3-methoxy-4-hydroxyphenylpyruvate
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competitive
3-thienylpyruvate
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mechanism-based inhibitor
4-(2,4-dichlorobenzyl)-1,3-dimethyl-5-hydroxypyrazole
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4-(3-cyclohexylpropanoyl)-5-hydroxy-2,2,6,6-tetramethylcyclohex-4-ene-1,3-dione
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4-(3-cyclohexylpropanoyl)-5-hydroxy-2,2,6-trimethyl-6-(3-methylbut-2-enyl)cyclohex-4-ene-1,3-dione
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4-(3-cyclohexylpropanoyl)-5-methoxy-2,2,6,6-tetramethylcyclohex-4-ene-1,3-dione
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4-(cyclohexanecarbonyl)-5-hydroxy-2,2,6,6-tetramethylcyclohex-4-ene-1,3-dione
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4-acetyl-5-hydroxy-2,2,6,6-tetramethylcyclohex-4-ene-1,3-dione
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4-aminophenylpyruvate
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competitive
4-decanoyl-5-hydroxy-2,2,6,6-tetramethylcyclohex-4-ene-1,3-dione
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4-dodecanoyl-5-hydroxy-2,2,6,6-tetrakis(3-methylbut-2-enyl)cyclohex-4-ene-1,3-dione
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4-dodecanoyl-5-hydroxy-2,2,6,6-tetramethylcyclohex-4-ene-1,3-dione
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4-hexanoyl-5-hydroxy-2,2,6,6-tetramethylcyclohex-4-ene-1,3-dione
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4-hydroxybenzaldehyde
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50% inhibition above 10 mM, noncompetitive
4-hydroxyphenylpyruvate
4-hydroxytetrafluorophenylpyruvate
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mechanism-based inhibitor
5-hydroxy-2,2,6,6-tetramethyl-4-(2-methylbutanoyl)cyclohex-4-ene-1,3-dione
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-
5-hydroxy-2,2,6,6-tetramethyl-4-(2-phenylacetyl)cyclohex-4-ene-1,3-dione
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5-hydroxy-2,2,6,6-tetramethyl-4-(3-methylbutanoyl)cyclohex-4-ene-1,3-dione
-
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5-hydroxy-2,2,6,6-tetramethyl-4-(3-phenylpropanoyl)cyclohex-4-ene-1,3-dione
-
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5-hydroxy-2,2,6,6-tetramethyl-4-palmitoylcyclohex-4-ene-1,3-dione
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5-hydroxy-4-isobutyryl-2,2,6,6-tetrakis(3-methylbut-2-enyl)cyclohex-4-ene-1,3-dione
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5-hydroxy-4-isobutyryl-2,2,6,6-tetramethylcyclohex-4-ene-1,3-dione
-
-
8-Hydroxyquinoline-5-sulfonic acid
-
560 nM, 50% inhibition
Acetopyruvate
-
0.33 mM, 50% inhibition, competitive
Al3+
10 mM, 7% inhibition
Bathocuproine
-
3 mM, 50% inhibition
bathophenanthroline
benzobicyclon hydrolysate
-
Ca2+
10 mM, 16% inhibition
Co2+
10 mM, 32% inhibition
Cu2+
10 mM, complete inhibition
Cupferron
diethyl dicarbonate
-
5 mM, 50% inhibition
diethyldithiocarbamate
diketonitrile of isoxaflutole
-
half-site reactivity, nearly irreversible
Dithizone
DL-3,4-dihydroxyphenylalanine
-
0.32 mM, 50% inhibition, noncompetitive
DL-4-hydroxyphenyllactate
-
50% inhibition above 10 mM, competitive
DL-Epinephrine
-
0.17 mM, 50% inhibition, noncompetitive
DTT
10 mM, 61% inhibition
ethanol
-
5% v/v, 50% inhibition, complete loss of activity at 20% v/v
Fe2+-chelators
-
-
-
homogentisate
K+
10 mM, 6% inhibition
L-Phe
-
10 mM, 50% inhibition, competitive
LnCl3
-
1 mM, 50% inhibition
-
mesotrione
-
binding constant of 602 microM
Mg2+
10 mM, 18% inhibition
Mn2+
10 mM, 97% inhibition
Na+
10 mM, 14% inhibition
Ni2+
10 mM, 28% inhibition
o-hydroxyphenylpyruvate
-
competitive inhibitor of 4-hydroxyphenylpyruvate
oxaloacetate
-
10 mM, 50% inhibition, noncompetitive
pentafluorophenylpyruvate
-
competitive
phenylglyoxalate
-
50% inhibition above 10 mM, competitive
phenylpyruvate
pyridoxal 5'-phosphate
-
2 mM, 50% inhibition
pyruvate
-
50% inhibition above 10 mM, competitive
SDS
2% (w/v), complete inhibition
sulcotrione
for protein expressed in Escherichia coli DH5alpha (inhibition assayed without preincubation): 0 micoM sulcotrione = 100% activity, 0.5 microM sulcotrione = 58% activity left, 1.0 microM sulcotrione = 21.3% activity left, 1.5 microM sulcotrione = 2.8% activity left. Preincubation of the enzyme expressed in Escherichia coli SG13009 with sulcotrione for 15 min, significantly enhances the inhibition from 40% (1 microM sulcotrione/no preincubation) to 10% (1 microM sulcotrione/15 min preincubation).
thiophenol oxalate
-
-
thiophenyl oxalate
-
competitive
Tiron
-
0.4 mM, 50% inhibition
topramezone
-
-
trans-4-hydroxycinnamate
-
50% inhibition above 10 mM, competitive
triketone-rich fraction
-
-
Urea
1 M, 3% inhibition. 3 M, 42% inhibition. 5 M, 56% inhibition
YCl3
-
1 mM, 50% inhibition
Zn2+
10 mM, 65% inhibition
[1-tert-butyl-3-(2,4-dichlorophenyl)-5-hydroxy-1H-pyrazol-4-yl][2-chloro-4-(methylsulfonyl)phenyl]methanone
-
50% inhibition at 12 nM
additional information
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-butanol
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5% v/v, 2.9fold activation
1-propanol
-
10% v/v, 2.1fold activation
2,6-dichlorophenol indophenol
acetone
-
10% v/v, 5.7fold activation
acetonitrile
-
10% v/v, 3.6fold activation
ascorbate
catalase
-
from bovine liver, required for activity
-
Cyclohexanol
-
5% v/v, 4.4fold activation
dioxane
-
10% v/v, 2.8fold activation
ethanol
-
10% v/v, 2fold activation
ether
-
10% v/v, 2.6fold activation
glutathione
-
reducing cofactor required, either ascorbate, or a combination of 2,6-dichlorophenol indophenol and glutathione in presence of catalase
methanol
-
10% v/v, 1.6fold activation
methyl-cellosolve
-
10% v/v, 2.2fold activation
tetrahydrofuran
-
10% v/v, 6.7fold activation
Trypsin
Frog
-
liver enzyme appears to be present in an inactive form which can be activated by treatment with trypsin or by autolysis
-
additional information
regarding expression and acitvity, rich or complex media (surplus of yeast extract, addition of glycerol and buffering of pH) are superior to media with less complex composition. Supplementation of media with FeSO4 or tyrosine does not substantially upgrade expression and activity levels.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.027
(4-hydroxyphenyl)-pyruvate
-
pH 7.0, 25C
0.5
2-thienylpyruvate
-
-
0.05
3,4-Dihydroxyphenylpyruvate
-
-
0.25
3-thienylpyruvate
-
-
0.0043 - 54
4-hydroxyphenylpyruvate
0.05
4-hydroxytetrafluorophenylpyruvate
0.069 - 0.1
O2
0.115
oxygen
-
activity is measured polarographically, assays include 0.5 microM of enzyme, 500 microM betaME, Fe2+ stoichiometric with enzyme, and 400 microM 4-hydroxyophenylpyruvate in 20 mM HEPES at pH 7.0 at 4C
0.06 - 0.52
phenylpyruvate
additional information
additional information
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
6.8
(4-hydroxyphenyl)-pyruvate
Streptomyces avermitilis
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-
0.03 - 9.9
4-hydroxyphenylpyruvate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.27 - 254
4-hydroxyphenylpyruvate
423
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0013
(2,6-difluoro-4-hydroxyphenyl)pyruvate
-
-
0.0000098
2-(2-chloro-4-methanesulfonylbenzoyl)-1,3-cyclohexanedione
-
-
0.4 - 1.9
4-hydroxyphenylpyruvate
0.014
pentafluorophenylpyruvate
-
-
0.15
thiophenol oxalate
-
-
additional information
additional information
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00675
4-(2,4-dichlorobenzyl)-1,3-dimethyl-5-hydroxypyrazole
Coptis japonica var. dissecta
A7BG64
recombinant enzyme
0.00017
4-(3-cyclohexylpropanoyl)-5-hydroxy-2,2,6,6-tetramethylcyclohex-4-ene-1,3-dione
Arabidopsis thaliana
-
-
0.00227
4-(3-cyclohexylpropanoyl)-5-hydroxy-2,2,6-trimethyl-6-(3-methylbut-2-enyl)cyclohex-4-ene-1,3-dione
Arabidopsis thaliana
-
-
0.00041
4-(3-cyclohexylpropanoyl)-5-methoxy-2,2,6,6-tetramethylcyclohex-4-ene-1,3-dione
Arabidopsis thaliana
-
-
0.000019
4-decanoyl-5-hydroxy-2,2,6,6-tetramethylcyclohex-4-ene-1,3-dione
Arabidopsis thaliana
-
-
0.00025
4-dodecanoyl-5-hydroxy-2,2,6,6-tetramethylcyclohex-4-ene-1,3-dione
Arabidopsis thaliana
-
-
0.00096
4-hexanoyl-5-hydroxy-2,2,6,6-tetramethylcyclohex-4-ene-1,3-dione
Arabidopsis thaliana
-
-
0.0143
5-hydroxy-2,2,6,6-tetramethyl-4-(2-methylbutanoyl)cyclohex-4-ene-1,3-dione
Arabidopsis thaliana
-
-
0.0189
5-hydroxy-2,2,6,6-tetramethyl-4-(2-phenylacetyl)cyclohex-4-ene-1,3-dione
Arabidopsis thaliana
-
-
0.0118
5-hydroxy-2,2,6,6-tetramethyl-4-(3-methylbutanoyl)cyclohex-4-ene-1,3-dione
Arabidopsis thaliana
-
-
0.00075
5-hydroxy-2,2,6,6-tetramethyl-4-(3-phenylpropanoyl)cyclohex-4-ene-1,3-dione
Arabidopsis thaliana
-
grandiflorone, most active naturally occurring beta-triketone
0.00031
5-hydroxy-2,2,6,6-tetramethyl-4-palmitoylcyclohex-4-ene-1,3-dione
Arabidopsis thaliana
-
-
0.0445
5-hydroxy-4-isobutyryl-2,2,6,6-tetramethylcyclohex-4-ene-1,3-dione
Arabidopsis thaliana
-
-
0.00234
benzobicyclon hydrolysate
Coptis japonica var. dissecta
A7BG64
recombinant enzyme
0.000015 - 0.000023
topramezone
additional information
3,3,5,5-tetramethyl-2,4,6-trioxocyclohexyl 3-methylbutanoate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.004
protein expressed in Escherichia coli DH5alpha
0.04
purified recombinant mutant R378K, pH 6.5, 37C, homogentisate production
0.06
purified recombinant mutant E254D, pH 6.5, 37C, O2 consumption
0.07
purified recombinant mutant R378K, pH 6.5, 37C, O2 consumption
0.11 - 0.2
protein expressed in Escherichia coli SG13009
0.17 - 0.26
protein expressed in Escherichia coli M15(pRep4)
0.2
purified recombinant mutant E254D, pH 6.5, 37C, homogentisate production
0.51 - 1.1
-
enzyme forms 1, 2, and 3
0.6 - 0.9
-
-
2.6
purified recombinant wild-type enzyme, pH 6.5, 37C, O2 consumption
2.8
purified recombinant wild-type enzyme, pH 6.5, 37C, homogentisate production
10.6
-
pH 7.0, 25C
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4
two pH optima are observed at 50C: pH 4.0 (close to native conditions, narrow maximum) and pH 7.0 (broad maximum)
4.5
-
and a second optimum at pH 7.8
4.6
-
and a second optimum at pH 7.4, enzyme form 3
5.1
-
and a second optimum at pH 7.4, enzyme form 1 and 2
7.3
-
-
7.4
-
and a second optimum at pH 5.1 for enzyme form 1 and 2, and at pH 4.6 for enzyme form 3
7.8
-
and a second optimum at pH 4.5
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 7
-
reaction rate is constant between pH 5 and pH 7
5.5 - 7.7
-
pH 5.5: about 50% of maximal activity, pH 7.7: about 55% of maximal activity
6 - 9.5
-
pH 6.0: about 55% of maximal activity, pH 9.5: about 50% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
maximal activity when assayed at pH 4.0 or 7.0
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 70
30C: about 65% of maximal activity, 70C: about 30% of maximal activity, assayed at pH 7.0
40 - 60
40C: about 55% of maximal activity, 60C: about 40% of maximal activity, assayed at pH 4.0
additional information
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
abundantly expressed in neurons of
Manually annotated by BRENDA team
-
-
Automatic Mining of ENzyme DAta
abundantly expressed in neurons of
Manually annotated by BRENDA team
-
etiolated
Manually annotated by BRENDA team
additional information