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1.13.11.27: 4-hydroxyphenylpyruvate dioxygenase

This is an abbreviated version!
For detailed information about 4-hydroxyphenylpyruvate dioxygenase, go to the full flat file.

Word Map on EC 1.13.11.27

Reaction

4-hydroxyphenylpyruvate
+
O2
=
homogentisate
+
CO2

Synonyms

4-HPPD, 4-hydroxyphenylpyruvare dioxygenase, 4-hydroxyphenylpyruvate dioxygenase, 4-hydroxyphenylpyruvic acid dioxygenase, 4HPPD, ASJ32_19370, At-HPPD, AtHPPD, AvHPPD-03, EC 1.14.2.2, EC 1.99.1.14, formerly, F Alloantigen, F protein, F-antigen homolog, HPD, hpdA, HPPD, HPPDase, Legiolysin, MsHPPD, oxygenase, 4-hydroxyphenylpyruvate di-, p-hydroxyphenyl pyruvate dioxygenase, p-hydroxyphenylpyruvate dioxygenase, p-hydroxyphenylpyruvate hydroxylase, p-hydroxyphenylpyruvate oxidase, p-hydroxyphenylpyruvic acid hydroxylase, p-hydroxyphenylpyruvic hydroxylase, p-hydroxyphenylpyruvic oxidase, PTO1369, Pt_Hpd, T-cell reactive protein, TF-AG, YS103B

ECTree

     1 Oxidoreductases
         1.13 Acting on single donors with incorporation of molecular oxygen (oxygenases)
             1.13.11 With incorporation of two atoms of oxygen
                1.13.11.27 4-hydroxyphenylpyruvate dioxygenase

Activating Compound

Activating Compound on EC 1.13.11.27 - 4-hydroxyphenylpyruvate dioxygenase

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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-butanol
-
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
-