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.

Reaction

4-hydroxyphenylpyruvate
+
O2
=
homogentisate
+
CO2

Synonyms

4-HPPD, 4-hydroxyphenylpyruvare dioxygenase, 4-hydroxyphenylpyruvate dioxygenase, 4-hydroxyphenylpyruvic acid dioxygenase, 4HPPD, 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

Engineering

Engineering on EC 1.13.11.27 - 4-hydroxyphenylpyruvate dioxygenase

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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
N261D
-
site-directed mutagenesis, during the reaction mechanism, the last 1,2 rearrangement is blocked in S246A HPPD mutant, so that an arene oxide-derived intermediate is released as an alternative product, the mutant shows increased Km and reduced kcat for 4-hydroxyphenylpyruvate compared to the wild-type enzyme
Q272E
-
site-directed mutagenesis, the mutant shows increased Km and reduced kcat for 4-hydroxyphenylpyruvate compared to the wild-type enzyme
Q286E
-
site-directed mutagenesis, the mutant shows increased Km and reduced kcat for 4-hydroxyphenylpyruvate compared to the wild-type enzyme
Q358E
-
site-directed mutagenesis, the mutant shows increased Km and reduced kcat for 4-hydroxyphenylpyruvate compared to the wild-type enzyme
S246A
-
site-directed mutagenesis, during the reaction mechanism, the last 1,2 rearrangement is blocked in S246A HPPD mutant, so that an arene oxide-derived intermediate is released as an alternative product, the mutant shows increased Km and reduced kcat for 4-hydroxyphenylpyruvate compared to the wild-type enzyme
N275D
-
site-directed mutagenesis
Q286E
-
site-directed mutagenesis
Q300E
-
site-directed mutagenesis
Q372E
-
site-directed mutagenesis
S260A
-
site-directed mutagenesis
E254D
-
site-directed mutagenesis, the mutant shows 5% remaining activity compared to the wild-type enzyme
Q375N
-
site-directed mutagenesis, the mutant shows that a solvent accessible channel opens to the putative substrate binding site, suggesting this is responsible for the complete loss of activity, modeling, overview. Inactive mutant
Q375N/R378K
-
site-directed mutagenesis, inactive mutant
R378K
-
site-directed mutagenesis, the mutant shows 5% remaining activity compared to the wild-type enzyme
P214T
-
site-directed mutagenesis, during hte reaction mechanism, the last 1,2 rearrangement is blocked in S246A HPPD mutant, so that an arene oxide-derived intermediate is released as an alternative product
F337I
-
0.67 of wild-type activity
F341Y
-
16.9% of wild-type activity
F364I
-
site-directed mutagenesis, the mutant enzyme produces 47% homogentisate, 15% 4-hydroxyphenylacetate, and 19% quinolacetate, which differs from the wild-type activity
N216I
-
0.15% of wild-type activity
N216I/F337I
-
inactive
N216I/F337I/F341Y
-
inactive
N216I/F341Y
-
inactive
N245D
-
site-directed mutagenesis, the mutant enzyme produces 52% homogentisate and 26.8% 4-hydroxyphenylacetate, and 21.2% quinolacetate, which differs from the wild-type activity
N245I
-
site-directed mutagenesis, the mutant enzyme produces 13% homogentisate and 87% 4-hydroxyphenylacetate, which differs from the wild-type activity
P214T
-
1.6% of wild-type activity
P214T/F337I/F341Y
-
inactive
P214T/N216I
-
inactive
P214T/N216I/F337I
-
inactive
P214T/N216I/F337I/F341Y
-
inactive
P214T/N216I/F341Y
-
inactive
N245S
-
site-directed mutagenesis, the mutant produces quinolacetic acid as reaction product
-
additional information