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
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1.13.11.27
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syncytial
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viruses
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newcastle
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hn
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paramyxovirus
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epitope
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hemagglutinin-neuraminidase
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infant
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measles
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parainfluenza
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herbicide
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sendai
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homogentisate
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heptad
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hemagglutinin
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virion
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fusogenic
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tyrosinemia
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metapneumovirus
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prefusion
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anti-f
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palivizumab
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weed
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postfusion
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paramyxoviridae
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furin
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distemper
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ectodomains
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mumps
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virus-cell
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rsv-infected
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six-helix
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cleavability
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formalin-inactivated
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lasota
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virus-neutralizing
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virus-like
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morbillivirus
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panencephalitis
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ntbc
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anti-rsv
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nipah
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velogenic
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nucleopolyhedrovirus
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drug development
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alkaptonuria
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diagnostics
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thomsen-friedenreich
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agriculture
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environmental protection
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rinderpest
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live-attenuated
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medicine
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merger
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fumarylacetoacetate
- 1.13.11.27
-
syncytial
- viruses
- newcastle
- hn
- paramyxovirus
- epitope
- hemagglutinin-neuraminidase
- infant
- measles
- parainfluenza
-
herbicide
-
sendai
- homogentisate
-
heptad
- hemagglutinin
- virion
-
fusogenic
- tyrosinemia
- metapneumovirus
-
prefusion
-
anti-f
-
palivizumab
-
weed
-
postfusion
- paramyxoviridae
- furin
- distemper
- ectodomains
- mumps
-
virus-cell
-
rsv-infected
-
six-helix
-
cleavability
-
formalin-inactivated
-
lasota
-
virus-neutralizing
-
virus-like
- morbillivirus
- panencephalitis
- ntbc
-
anti-rsv
-
nipah
-
velogenic
- nucleopolyhedrovirus
- drug development
- alkaptonuria
- diagnostics
-
thomsen-friedenreich
- agriculture
- environmental protection
- rinderpest
-
live-attenuated
- medicine
-
merger
- fumarylacetoacetate
Reaction
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
1.13.11.27 4-hydroxyphenylpyruvate dioxygenaseAdvanced search results
results (
results (Engineering
Engineering on EC 1.13.11.27 - 4-hydroxyphenylpyruvate dioxygenase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
L119P
mutation increases the thermostability of the enzyme
P103Q
mutation increases the thermostability of the enzyme
P103Q/L119P
mutation enables recombinant Escherichia coli strains to form melanin at 30°C and 37°C
P117L
Escherichia coli cells expressing the mutant form pigment at all tested temperatures
Q101P
Escherichia coli cells expressing the mutant fail to form pigment at all 37°C
Q101P/P117L
Escherichia coli cells expressing the mutant form pigment at all tested temperatures
S18T
mutation increases the thermostability of the enzyme
S18T/L119P
mutation enables recombinant Escherichia coli strains to form melanin at 30°C
S18T/P103Q
mutation enables recombinant Escherichia coli strains to form melanin at 30°C and 37°C
S18T/P103Q/L119P
mutation enables recombinant Escherichia coli strains to form melanin at 30°C and 37°C
T16S
Escherichia coli cells expressing the mutant form pigment at all tested temperatures
T16S/P117L
Escherichia coli cells expressing the mutant form pigment at all tested temperatures
T16S/Q101P
Escherichia coli cells expressing the mutant form pigment at all tested temperatures
T16S/Q101P/P117L
Escherichia coli cells expressing the mutant completely lose melanin formation ability at 30°C and 37°C
M335H/P336A/E363Q
residues 336 and 363 are substituted by the corresponding residues of Zea mays HPPD, more than twofold increase in IC50 for sulcotrione and tembotrione. Increased herbicide tolerance compared to wild-type matches with a clear shift in the free energy profile toward favoring the closed helix H11 state
M335H/P336A/P339T/T341D/E363Q/E426Q
substitutions correspond to residues found in Zea mays. The mutant has a clear preference for the closed H11 state
N261D
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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
P315R/R328A/L347M
mutations induce an 8fold increase in the value of k4 in respect of mesotrione
Q272E
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site-directed mutagenesis, the mutant shows increased Km and reduced kcat for 4-hydroxyphenylpyruvate compared to the wild-type enzyme
Q286E
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site-directed mutagenesis, the mutant shows increased Km and reduced kcat for 4-hydroxyphenylpyruvate compared to the wild-type enzyme
Q358E
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site-directed mutagenesis, the mutant shows increased Km and reduced kcat for 4-hydroxyphenylpyruvate compared to the wild-type enzyme
S246A
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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
E254D
site-directed mutagenesis, the mutant shows 5% remaining activity compared to the wild-type enzyme
L224A
binding ability of the mutant to nitisinone is significantly weaker than that of wild-type
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
R378K
site-directed mutagenesis, the mutant shows 5% remaining activity compared to the wild-type enzyme
Y221A
binding ability of the mutant to nitisinone is significantly weaker than that of wild-type
P214T
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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
synthesis
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recombinant Escherichia coli expression HppD can produce pyomelanin at levels up to 315.5 mg/l (13.1 mg/l/h) in 24 h. Highest pyomelanin production is achieved when L-tyrosine and 0.5mM Cu2+ are supplemented into LB medium
E322R
Sphingobium sp. TPM-19
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mutant shows improved resistance to topramezone, with about 98% of wild-type activity, and displays increased resistance to mesotrione
K249R
Sphingobium sp. TPM-19
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mutant shows improved resistance to topramezone, with about 98% of wild-type activity, and displays increased resistance to mesotrione and DKN, i.e. the active ingredient of isoxaflutole
F364I
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site-directed mutagenesis, the mutant enzyme produces 47% homogentisate, 15% 4-hydroxyphenylacetate, and 19% quinolacetate, which differs from the wild-type activity
N245D
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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
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site-directed mutagenesis, the mutant enzyme produces 13% homogentisate and 87% 4-hydroxyphenylacetate, which differs from the wild-type activity
N245Q
N245S
P243T
S230A
N245S
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site-directed mutagenesis, the mutant produces quinolacetic acid as reaction product
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M335H/P336A/E363Q
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residues 336 and 363 are substituted by the corresponding residues of Zea mays HPPD, more than twofold increase in IC50 for sulcotrione and tembotrione. Increased herbicide tolerance compared to wild-type matches with a clear shift in the free energy profile toward favoring the closed helix H11 state
M335H/P336A/P339T/T341D/E363Q/E426Q
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substitutions correspond to residues found in Zea mays. The mutant has a clear preference for the closed H11 state
additional information
N245Q
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site-directed mutagenesis, the mutant enzyme produces 44.5% homogentisate and 52% 4-hydroxyphenylacetate, and 4% quinolacetate, which differs from the wild-type activity
N245Q
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site-directed mutagenesis, the mutant enzyme produces 52% homogentisate and 45% 4-hydroxyphenylacetate, and 3% quinolacetate, which differs from the wild-type activity
N245S
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site-directed mutagenesis, the mutant enzyme produces 3.4% homogentisate and 6.6% 4-hydroxyphenylacetate, and 90% quinolacetate, which differs from the wild-type activity
N245S
site-directed mutagenesis, the mutant produces quinolacetic acid as reaction product
P243T
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site-directed mutagenesis, the mutant enzyme produces 13% homogentisate, 8.7% 4-hydroxyphenylacetate, and 78% quinolacetate, which differs from the wild-type activity
P243T
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site-directed mutagenesis, the mutant enzyme produces 8.4% homogentisate, 46.5% 4-hydroxyphenylacetate, and 45% quinolacetate, which differs from the wild-type activity
S230A
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site-directed mutagenesis, the mutant enzyme produces 11.6% homogentisate, 30.6% 4-hydroxyphenylacetate, and 57.8% quinolacetate, which differs from the wild-type activity
S230A
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site-directed mutagenesis, the mutant enzyme produces 7% homogentisate, 57% 4-hydroxyphenylacetate, and 36% quinolacetate, which differs from the wild-type activity
additional information
human 4-HPPD possesses an extended C-terminus compared to other 4-HPPD enzymes. Successive truncation of the disordered tail which follows the final alpha-helix results in no changes in the Km value for 4-HPP substrate but the kcat values are significantly reduced by ca. 25 to 50%. The different conformation of E254, R378 and Q375 in the final helix might be the cause of the activity loss
additional information
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human 4-HPPD possesses an extended C-terminus compared to other 4-HPPD enzymes. Successive truncation of the disordered tail which follows the final alpha-helix results in no changes in the Km value for 4-HPP substrate but the kcat values are significantly reduced by ca. 25 to 50%. The different conformation of E254, R378 and Q375 in the final helix might be the cause of the activity loss
additional information
construction of a nanobiosensor based on HPPD for mesotrione detection. The atomic force microscope tip functionalization with HPPD immobilized in self-assembled monolayers is confirmed by fluorescence microscopy and atomic force spectroscopy. The cross-linker N-(3-dimethylaminopropyl)-N-ethylcarbodiimide hydrochloride is responsible for properly preserving the enzyme on the tip
additional information
upon removal of the 12 N-terminal residues, the kcat/Km decreases 8fold compared to wild-type. The wild-type level of activity is retained in a mutant missing the 17 N-terminal residues, with a kcat/Km 11fold higher than that of the mutant lacking 12 N-terminal residues, however, the structural stability of this mutant is lower than that of wild type
additional information
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upon removal of the 12 N-terminal residues, the kcat/Km decreases 8fold compared to wild-type. The wild-type level of activity is retained in a mutant missing the 17 N-terminal residues, with a kcat/Km 11fold higher than that of the mutant lacking 12 N-terminal residues, however, the structural stability of this mutant is lower than that of wild type
additional information
heterologous overexpression of gene MsHPPD in Arabidopsis thaliana significantly increases the level of beta-tocotrienol and the total vitamin E content in Arabidopsis seeds. The transgenic Arabidopsis seeds exhibit an accelerated germination time, compared with wild-type seeds under normal conditions, as well as under NaCl and abscisic acid treatments. The expression level of several genes associated with abscisic acid biosynthesis (NCED3, NCED5, and NCED9) and the abscisic acid signaling pathway (RAB18, ABI3, and ABI5) are significantly downregulated in MsHPPD-overexpressing transgenic lines, as well as the total free abscisic acid content, phenotype. MsHPPD expression in three MsHPPD-overexpressing transgenic lines and wild-type, overview. Expression levels of ABA biosynthesis and ABA signaling pathway genes in MsHPPD-overexpressing transgenic Arabidopsis thaliana
additional information
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heterologous overexpression of gene MsHPPD in Arabidopsis thaliana significantly increases the level of beta-tocotrienol and the total vitamin E content in Arabidopsis seeds. The transgenic Arabidopsis seeds exhibit an accelerated germination time, compared with wild-type seeds under normal conditions, as well as under NaCl and abscisic acid treatments. The expression level of several genes associated with abscisic acid biosynthesis (NCED3, NCED5, and NCED9) and the abscisic acid signaling pathway (RAB18, ABI3, and ABI5) are significantly downregulated in MsHPPD-overexpressing transgenic lines, as well as the total free abscisic acid content, phenotype. MsHPPD expression in three MsHPPD-overexpressing transgenic lines and wild-type, overview. Expression levels of ABA biosynthesis and ABA signaling pathway genes in MsHPPD-overexpressing transgenic Arabidopsis thaliana
additional information
construction and complementation of melA mutants of Shewanella oneidensis MR-1, in-frame deletion mutagenesis
additional information
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construction and complementation of melA mutants of Shewanella oneidensis MR-1, in-frame deletion mutagenesis
additional information
Shewanella oneidensis MR-1 / ATCC 700550
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construction and complementation of melA mutants of Shewanella oneidensis MR-1, in-frame deletion mutagenesis
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